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X-WR-CALDESC:Events for Center for RNA Biomedicine
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BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210407T160000
DTEND;TZID=America/Detroit:20210407T170000
DTSTAMP:20260504T112159
CREATED:20210104T143303Z
LAST-MODIFIED:20210127T001017Z
UID:7657-1617811200-1617814800@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: Bay Area RNA Club (BARC)
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-bay-area-rna-club-barc/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210419T160000
DTEND;TZID=America/Detroit:20210419T170000
DTSTAMP:20260504T112159
CREATED:20210128T141644Z
LAST-MODIFIED:20210310T212447Z
UID:7864-1618848000-1618851600@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Jailson (Jay) Brito Querido\, MRC Laboratory of Molecular Biology
DESCRIPTION:“Structural insights into mRNA translation initiation in humans”\nJailson (Jay) Brito Querido\, Ph.D.\nPostdoctoral Scientist\nMRC Laboratory of Molecular Biology\nCambridge\, UK \nZOOM \nFLYER IN PDF \nREGISTRATION REQUIRED: https://umich.zoom.us/webinar/register/WN_78YYOhIhTbOBy2_JSdM7Wg \nABSTRACT: A key step in translational initiation is the recruitment of the 43S pre-initiation complex (43S PIC) by the cap-binding complex (eIF4F) at the 5´ end of mRNA. Eukaryotic initiation factors eIF1\, eIF1A\, eIF3\, eIF5\, and the ternary complex (TC) of eIF2–GTP–tRNAiMet bind to the 40S ribosomal subunit to form the 43S PIC. Once assembled\, the 43S PIC is recruited to the cap-binding complex eIF4F at the 5´end of mRNA to form a 48S initiation complex (48S). The 48S then scans along the mRNA to locate a start codon. To understand the mechanisms involved\, we determined the structure of a reconstituted human 48S using cryo-electron microscopy. The structure reveals insights into early events of translation initiation complex assembly. It reveals how eIF4F interacts with subunits of the eIF3 structural core near the mRNA exit channel in the 43S. The location of eIF4F is consistent with a slotting model of mRNA recruitment and suggests a “blind-region” that would preclude recognition of start sites upstream of the location of the P site at the point of recruitment. \nKEYWORDS: mRNA\, ribosome\, eIF4F\, eIF4A\, translation
URL:https://rna.umich.edu/events/jay-querido/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210421T090000
DTEND;TZID=America/Detroit:20210421T100000
DTSTAMP:20260504T112159
CREATED:20210104T143404Z
LAST-MODIFIED:20210415T215048Z
UID:7659-1618995600-1618999200@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: Shanghai RNA Club
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-tba-host-4/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210503T160000
DTEND;TZID=America/Detroit:20210503T170000
DTSTAMP:20260504T112159
CREATED:20210126T234652Z
LAST-MODIFIED:20210413T174229Z
UID:7841-1620057600-1620061200@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Olivia Rissland\, University of Colorado School of Medicine
DESCRIPTION:“Regulating the Regulators: Control of RNA Binding Proteins during Embryogenesis”\nOlivia Rissland\, Ph.D.\nAssistant Professor\nRNA Bioscience Initiative | Department of Biochemistry & Molecular Genetics\nUniversity of Colorado School of Medicine \nZOOM \nREGISTRATION REQUIRED: https://umich.zoom.us/webinar/register/WN_vA9zYS5nSEenf8Zmt1f-qA \nFLYER IN PDF \n  \nABSTRACT: The maternal-to-zygotic transition (MZT) is a conserved step in animal development\, where control is passed from the maternal to the zygotic genome. Although the MZT is typically considered from its impact on the transcriptome\, we previously found that three maternally deposited Drosophila RNA binding proteins (ME31B\, Trailer Hitch [TRAL]\, and Cup) are also cleared during the MZT by unknown mechanisms. Here\, we show that these proteins are degraded by the ubiquitin-proteasome system. Marie Kondo\, an E2 conjugating enzyme\, and the E3 CTLH ligase are required for the destruction of ME31B\, TRAL\, and Cup. Structure modeling of the Drosophila CTLH complex suggests that substrate recognition is different than orthologous complexes. Despite occurring hours earlier\, egg activation mediates clearance of these proteins through the Pan Gu kinase\, which stimulates translation of Kondo mRNA. Clearance of the maternal protein dowry thus appears to be a coordinated\, but as-yet underappreciated\, aspect of the MZT.
URL:https://rna.umich.edu/events/olivia-rissland/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210504T150000
DTEND;TZID=America/Detroit:20210504T160000
DTSTAMP:20260504T112159
CREATED:20210416T182959Z
LAST-MODIFIED:20210416T182959Z
UID:8551-1620140400-1620144000@rna.umich.edu
SUMMARY:Seminar: Tatjana Trcek\, Johns Hopkins University
DESCRIPTION:Zoom link \n“RNA Granules: A View from the RNA Perspective”\nTatjana Trcek\, PhD\nAssistant Professor\nDepartment of Biology\nJohns Hopkins University\n  \nHosted by:\nStephanie Moon\, Ph.D.\nAssistant Professor of Human Genetics\nFaculty Scholar of the Center for RNA Biomedicine\nAffiliate Faculty\, Biological Chemistry\nFLYER IN PDF \nDepartment of Human Genetics Seminar \n  \n 
URL:https://rna.umich.edu/events/seminar-tatjana-trcek-johns-hopkins-university/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210505T090000
DTEND;TZID=America/Detroit:20210505T100000
DTSTAMP:20260504T112159
CREATED:20210104T143436Z
LAST-MODIFIED:20210426T152958Z
UID:7661-1620205200-1620208800@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: Cambridge RNA Club
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-tba-host-5/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210517T160000
DTEND;TZID=America/Detroit:20210517T170000
DTSTAMP:20260504T112159
CREATED:20210126T235922Z
LAST-MODIFIED:20210512T200602Z
UID:7845-1621267200-1621270800@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Thomas Martinez\, Salk Institute for Biological Studies
DESCRIPTION:“Annotation and Characterization of Human Protein-coding Small Open Reading Frames”\nThomas Martinez\, Ph.D.\nPostdoctoral Fellow\nSalk Institute for Biological Studies \nZOOM \nREGISTRATION REQUIRED:\nhttps://umich.zoom.us/webinar/register/WN_90RkcQTGQZa7ifQ8kbSdNQ \nFLYER IN PDF \nKEYWORDS: microprotein\, smORF\, ribosome profiling \nABSTRACT: Functional protein-coding small open reading frames (smORFs) are emerging as an important class of genes. Several smORF-encoded microproteins have been characterized and implicated in a variety of critical processes\, including regulation of mRNA decay\, DNA repair\, and muscle formation. Thus\, rigorous and comprehensive annotation of protein-coding smORFs is critical to our understanding of basic biology and physiology\, as well as disease. We recently developed an improved workflow that integrates de novo transcriptome assembly and ribosome profiling to overcome obstacles with previous methods to more confidently annotate thousands of novel smORFs across multiple human cell lines\, including hundreds encoded on putative non-coding RNAs. Over 1\,500 smORFs are found in two or more cell lines\, and ~40% lack a canonical AUG start codon. Evolutionary conservation analyses suggest that hundreds of smORF-encoded microproteins are likely functional. We also find that smORF-derived peptides are detectable on human leukocyte antigen complexes\, positioning smORFs as a source of novel antigens. The annotation of protein-coding smORFs radically alters the current view of the human genome’s coding capacity and will provide a rich pool of unexplored\, functional human genes. \nBIOGRAPHY: Thomas received his B.S. in Biological Engineering from MIT and trained in Prof. JoAnne Stubbe’s laboratory\, where he studied the mechanism of ribonucleotide reductase. He then received his Ph.D. in Biochemistry & Molecular Biophysics from Caltech as an NIH NRSA predoctoral fellow under the mentorship of Prof. Peter Dervan. His thesis work focused primarily on characterizing the effects of DNA binding pyrrole-imidazole polyamides on DNA replication in prostate cancer cells. Thomas is currently an NIH NRSA postdoctoral fellow in Prof. Alan Saghatelian’s laboratory\, where he has developed an integrative platform combining ribosome profiling and de novo transcriptome assembly to discover functional smORF encoded microproteins in the human genome.
URL:https://rna.umich.edu/events/thomas-martinez/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210519T090000
DTEND;TZID=America/Detroit:20210519T100000
DTSTAMP:20260504T112159
CREATED:20210415T215014Z
LAST-MODIFIED:20210426T152937Z
UID:8528-1621414800-1621418400@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: Groupe de Recherche RNA (GDR)
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-groupe-de-recherche-rna-gdr/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210602T160000
DTEND;TZID=America/Detroit:20210602T170000
DTSTAMP:20260504T112159
CREATED:20210415T215152Z
LAST-MODIFIED:20210517T161826Z
UID:8534-1622649600-1622653200@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: European Molecular Biology Laboratory (EMBL)
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-tba/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210614T160000
DTEND;TZID=America/Detroit:20210614T170000
DTSTAMP:20260504T112159
CREATED:20210428T133100Z
LAST-MODIFIED:20210518T173059Z
UID:8623-1623686400-1623690000@rna.umich.edu
SUMMARY:RNA Innovation Seminar featuring Rising Scholars: Khan & McMillan
DESCRIPTION:Registration: https://umich.zoom.us/webinar/register/WN_uLz-ONHVQPuRINMYUNvBJQ \nFlyer: Khan & McMillan Seminar flyer \n\n“CCR5 as a model to examine reporter assays in evaluating translational phenomena”\nYousuf Khan\nKnight-Hennessy Scholar\nNSF fellow\nStanford University \n  \n  \n  \n  \nKeywords: dual luciferase\, frameshifting\, recoding\, CCR5 \nAbstract: During the decoding of a subset of mRNAs\, a proportion of ribosomes productively shift to the −1 reading frame at specific slippage-prone sites in a phenomenon known as programmed −1 ribosomal frameshifting (−1 PRF) to generate a frameshifted\, C-terminally unique protein. The first experimentally verified occurrence of functionally utilized non-retroelement derived −1 PRF in humans has been reported in the mRNA encoding the immune-functioning C-C chemokine receptor 5 (CCR5). Here\, we show that frameshifting does not occur during CCR5 decoding. Apart from its importance in understanding expression of a gene relevant to cancer\, an HIV-1 receptor (and the associated claimed rationale for generating the first humans derived from genetically modified embryos)\, the findings imply that caution is appropriate in assessing results from translational reporter assays. \n~and~\n“Intersection between RNA methylation and TDP43-mediated toxicity in ALS”\n \n  \nMike McMillan\nPh.D. candidate\nCellular and Molecular Biology\nUniversity of Michigan \n  \n  \n  \nKeywords: TDP43\, m6A\, ALS\, RNA stability \nAbstract: Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease resulting in the death of upper and lower motor neurons. ALS has no known cure and limited therapeutic options\, and the underlying pathological mechanisms remain unclear. Despite considerable variability in clinical presentation\, over 95% of ALS cases exhibit cytoplasmic inclusions of the RNA binding protein TDP43. Emerging evidence suggests that TDP43 is crucial for RNA stability\, and that dysregulation of RNA homeostasis may contribute to ALS pathogenesis.\nMethylation of RNA at the 6th position nitrogen (N6-methyladenosine methylation\, or m6A) by methyltransferases (writers) or removal of methyl groups by demethylases (erasers) has dramatic effects on RNA stability and translation mediated by a family of RNA biding proteins that recognize methylated RNA (readers). m6A writers and erasers specifically localize to nuclear speckles\, membraneless nuclear organelles rich in RNA binding proteins and splicing factors\, including TDP43. Together with our data showing that TDP43 regulates RNA stability\, these observations suggest that TDP43 may destabilize m6A modified RNA. Here\, we show that methylated RNA co-purified with TDP43 from cultured cells via RNA immunoprecipitation\, and abrogation of methylation sites disrupted TDP43 binding\, suggesting that TDP43 recognizes m6A modified RNA in cellulo. We also noted profound and widespread hypermethylation of coding and non-coding transcripts in ALS spinal cord\, many overlapping with confirmed TDP43 target transcripts. Consistent with a central role for m6A modification in TDP43-mediated toxicity\, we identified several factors operating within the m6A pathway that enhance or suppress the toxicity of TDP43 in rodent primary cortical neurons via a single-cell CRISPR/Cas9 candidate-based screen. Genetic knockout of the established m6A reader YTHDF2 rescued TDP43 toxicity in primary neurons\, and YTHDF2 was also upregulated in ALS postmortem sections. Together\, these data imply a fundamental link between m6A RNA modifications and ALS pathogenesis\, potentially mediated by TDP43-dependent RNA destabilization. \n 
URL:https://rna.umich.edu/events/rising-scholars-khan-mcmillan/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210616T160000
DTEND;TZID=America/Detroit:20210616T170000
DTSTAMP:20260504T112159
CREATED:20210415T215236Z
LAST-MODIFIED:20210517T161849Z
UID:8536-1623859200-1623862800@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: Yale Center for RNA Science and Medicine
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-tba-2/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210630T160000
DTEND;TZID=America/Detroit:20210630T170000
DTSTAMP:20260504T112159
CREATED:20210415T215318Z
LAST-MODIFIED:20210609T182833Z
UID:8538-1625068800-1625072400@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: University of Michigan
DESCRIPTION:REGISTRATION REQUIRED: https://umich.zoom.us/webinar/register/WN_6OEQ6sDAQ0-21GHm6d7VEQ\n\n“Dynamic multivalent interactions drive mammalian RNA regulation”\n \nSethu Pitchiaya\, Ph.D.\nDepartment of Urology \n\n  \n  \n  \n  \n  \n  \n  \n\n\n\n“Characterizing cellular RNA-protein interaction networks with chemical probes”\nChase Weidmann\, Ph.D.\nDepartment of Biological Chemistry \n  \n  \n  \n  \n  \n  \n  \n\nFor the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-pitchiaya-weidmann/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210714T090000
DTEND;TZID=America/Detroit:20210714T100000
DTSTAMP:20260504T112159
CREATED:20210415T215433Z
LAST-MODIFIED:20210415T215433Z
UID:8540-1626253200-1626256800@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: iRNA @ Istituto Italiano di Tecnologia (IIT)
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-irna-istituto-italiano-di-tecnologia-iit/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210728T090000
DTEND;TZID=America/Detroit:20210728T100000
DTSTAMP:20260504T112159
CREATED:20210415T215545Z
LAST-MODIFIED:20210426T152555Z
UID:8542-1627462800-1627466400@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: MD Anderson Center for RNA Interference and Non-Coding RNAs
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-md-anderson-center-for-rna-interference-and-non-coding-rnas/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210811T160000
DTEND;TZID=America/Detroit:20210811T170000
DTSTAMP:20260504T112159
CREATED:20210415T215644Z
LAST-MODIFIED:20210517T161927Z
UID:8544-1628697600-1628701200@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: RiboClub Sherbrooke
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host-tba-3/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20210825T090000
DTEND;TZID=America/Detroit:20210825T100000
DTSTAMP:20260504T112159
CREATED:20210415T215751Z
LAST-MODIFIED:20210426T152519Z
UID:8546-1629882000-1629885600@rna.umich.edu
SUMMARY:RNA Collaborative Seminar Series // Host: Institute of Molecular Biology (IMB)
DESCRIPTION:For the seminar details\, visit: https://www.rnasociety.org/rna-collaborative-seminar-series
URL:https://rna.umich.edu/events/rna-collaborative-seminar-series-host/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20211004T160000
DTEND;TZID=America/Detroit:20211004T170000
DTSTAMP:20260504T112159
CREATED:20210827T134403Z
LAST-MODIFIED:20210930T134032Z
UID:9267-1633363200-1633366800@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Byron Purse\, Ph.D.
DESCRIPTION:“Fluorescent nucleoside analogues with new properties”\nByron Purse\, Ph.D.\nAssociate Professor\nOrganic Chemistry\nSan Diego State University \n  \n  \n  \n  \nHYBRID SEMINAR:\nIn-person: Forum Hall\, Palmer Commons\nZoom: https://umich.zoom.us/webinar/register/WN__vvE2dtHQi-R3h05JUHBzQ \nFLYER IN PDF \nAbstract:\nFluorescent nucleoside analogues (FNAs) are powerful probes for studying the structure and dynamics of nucleic acids\, which are vital to understanding RNA function\, DNA damage repair\, nucleic acid–protein interactions\, regulatory mechanisms for gene expression\, and other aspects of nucleic acid function. Existing FNAs are prone to quenching by base pairing and stacking\, are clustered at the blue–green end of the visible spectrum\, and have limited brightness as compared with conventional fluorophores. Studies of nucleic acid function would benefit greatly from overcoming these limitations. We have designed\, synthesized\, and studied a series of fluorescent pyrimidine analogues\, aiming to address these limitations and develop a detailed understanding of the relationships between chemical structure and fluorescent responses to local environment in nucleic acids. Included in this series is a tricyclic cytidine analogue DEAtC that is nearly non-fluorescent as a nucleoside\, but responds to matched base pairing and stacking with a fluorescence turn-on. A chlorinated tricyclic cytidine 8-Cl-tCO reports on local environment by changes in the vibrational fine structure of its emission spectra. To address the problem of limited brightness\, we have design and synthesized a new NFA that we call ABN\, which has a conjugated push–pull system similar to those found in bright fluorophores such as rhodamines. ABN is the brightest known FNA when present in duplex nucleic acids\, and it is readily detected in single-molecule fluorescence measurements using both 1-photon and 2-photon excitation. Collectively\, these FNAs offer new capabilities for biophysical studies on nucleic acids. Comparisons of their structure and properties help to reveal mechanisms for fluorescence changes in response to local environment in nucleic acids.
URL:https://rna.umich.edu/events/byron-purse/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20211005T150000
DTEND;TZID=America/Detroit:20211005T160000
DTSTAMP:20260504T112159
CREATED:20210901T193912Z
LAST-MODIFIED:20210929T155531Z
UID:9346-1633446000-1633449600@rna.umich.edu
SUMMARY:Human Genetics Seminar: Rajesh Rao\, Ophthalmology & Visual Science\, U-M Medical School
DESCRIPTION:“Genetics through the Lens of an Ophthalmologist and Vision Scientist”\nRajesh C. Rao\, M.D.\nLeonard G. Miller Professor\nAssociate Professor\nDepartment of Ophthalmology & Visual Sciences\nDepartment of Pathology \n  \nDepartment of Human Genetics seminar\nZOOM MEETING ID: 947 5800 7294\nPASSCODE: 900076\nhttps://umich.zoom.us/j/94758007294?pwd=Sk9VMGlnTXRZWWJwbnZCZUx4MlI0QT09 \nFLYER IN PDF
URL:https://rna.umich.edu/events/rajesh-rao/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20211018T160000
DTEND;TZID=America/Detroit:20211018T170000
DTSTAMP:20260504T112159
CREATED:20210827T134441Z
LAST-MODIFIED:20210930T165005Z
UID:9269-1634572800-1634576400@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Tim Stasevich\, Ph.D.
DESCRIPTION:“Imaging single-mRNA translation dynamics in living color”\nTim Stasevich\, Ph.D.\nAssociate Professor\nDean and Pingping Tsao Professor of Biochemistry\nCSU Monfort Professor\nBoettcher Investigator\nColorado State University \nRegistration: https://umich.zoom.us/webinar/register/WN_OzTuwf2zRN-6zCZk1pA_lQ \n  \nFlyer in PDF \nKeywords:\ntranslational regulation\, gene expression\, fluorescence microscopy\, intrabodies\, single-molecule imaging \nAbstract:\nMy lab is creating technology to image mRNA translation in real time and with single-molecule precision in living cells. In this talk\, I will introduce our technology and describe how it can be used to amplify fluorescence from newly synthesized proteins as they are being translated from single mRNAs. I will show how we quantify these signals to determine the size\, shape\, subcellular localization\, and mobilities of mRNA translation sites\, as well as their protein synthesis dynamics. I will then highlight a few recent applications of our technology\, focusing mainly on a new biosensor we have developed to quantify how individual regulatory factors impact single mRNA translation dynamics. Using this biosensor\, we provide evidence that human Argonaute2 (Ago2) shuts down translation by down regulating translation initiation on the minutes timescale and helping usher translationally silent mRNAs into P-bodies on the hours timescale. I will conclude by discussing new fluorescent intrabodies my lab is engineering to light up nascent and mature proteins in multiple colors. As these intrabodies can be encoded on plasmids\, they can easily be adapted by other labs to image gene activity in diverse living systems. \nTimothy J. Stasevich is an Associate Professor in the Department of Biochemistry and Molecular Biology at Colorado State University (CSU). His lab uses a combination of advanced fluorescence microscopy\, genetic engineering\, and computational modeling to study the dynamics of gene regulation in living mammalian cells. His lab helped pioneer the imaging of real-time single-mRNA translation dynamics in living cells1. Dr. Stasevich received his B.S. in Physics and Mathematics from the University of Michigan\, Dearborn\, and his Ph. D. in Physics from the University of Maryland\, College Park. He transitioned into experimental biophysics as a post-doctoral research fellow in the laboratory of Dr. James G. McNally at the National Cancer Institute. During this time\, he developed technology based on fluorescence microscopy to help establish gold-standard measurements of live-cell protein dynamics. Dr. Stasevich next moved to Osaka University\, where he worked with Dr. Hiroshi Kimura as a Japan Society for the Promotion of Science Foreign Postdoctoral Research Fellow. While there\, he helped create technology to image endogenous proteins and their post-translation modifications in vivo. This allowed him to image the live-cell dynamics of epigenetic histone modifications during gene activation for the first time2. Before joining the faculty at CSU\, Dr. Stasevich spent a year as a Visiting Fellow at the HHMI Janelia Research Campus\, where he applied superresolution fluorescence microscopy to improve the spatiotemporal resolution of endogenous protein imaging in live cells. \n1. Morisaki\, T. et al. Real-time quantification of single RNA translation dynamics in living cells. Science 352\, 1425–1429 (2016).\n2. Stasevich\, T. J. et al. Regulation of RNA polymerase II activation by histone acetylation in single living cells. Nature 516\, 272–275 (2014).
URL:https://rna.umich.edu/events/tim-stasevich/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20211108T160000
DTEND;TZID=America/Detroit:20211108T170000
DTSTAMP:20260504T112159
CREATED:20210827T134511Z
LAST-MODIFIED:20211025T164624Z
UID:9271-1636387200-1636390800@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Zhonggang Hou & Jun Hee Lee
DESCRIPTION:“Harnessing diverse compact CRISPR-Cas3 for long-range genome engineering”\nZhonggang Hou\, Ph.D.\nResearch Investigator\nBiological Chemistry \nABSTRACT: Leading CRISPR-Cas technologies employ Cas9 and Cas12 enzymes that generate RNA-guided dsDNA breaks. Yet\, the most abundant microbial adaptive immune systems\, Type I CRISPR\, is under-exploited for eukaryotic application. I will discuss our effort on adopting the first minimal CRISPR-Cas3 from Neisseria Type I-C system\, to create targeted large chromosomal deletions in human cells. RNP delivery of the processive Cas3 nuclease and target recognition complex Cascade\, gave up to 90% editing efficiency. Unexpectedly\, Type I-C Cascade assembly in bacteria requires a previous unknown internal translation product Cas11 from within the cas8 gene. Our data show that expression of a separately encoded Cas11 is the key to enable plasmid- and mRNA- based editing in human cells. We demonstrate that “supplying cas11” is a universal strategy to harness divergent and streamlined Type I-C\, I-D and I-B editors with distinct PAM preferences and guide orthogonality. Our findings expand the CRISPR toolbox for long-range genome engineering. \nKEYWORDS: CRISPR; genome editing; Cascade; Cas3; Cas11; DNA targeting; crRNA; large deletion; Neisseria; genome engineering \n  \n  \n“Microscopic Examination of Spatial Transcriptome through Seq-Scope”\nJun Hee Lee\, Ph.D.\nAssociate Professor\nMolecular & Integrative Physiology \nKEYWORDS: Spatial Transcriptomics\, Seq-Scope \n  \nRegistration: https://umich.zoom.us/webinar/register/WN_qBK6mw7vQa6jOkZuS81_VQ \nFLYER IN PDF
URL:https://rna.umich.edu/events/zhonggang-hou-and-jun-hee-lee/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20211213T160000
DTEND;TZID=America/Detroit:20211213T170000
DTSTAMP:20260504T112159
CREATED:20210827T134607Z
LAST-MODIFIED:20211210T172017Z
UID:9275-1639411200-1639414800@rna.umich.edu
SUMMARY:RNA Faculty Candidate Seminar: Paul Donlin-Asp\, Max Planck Institute for Brain Research
DESCRIPTION:“Resolving the localisation and dynamics of mRNA and protein synthesis within neurons”\nPaul Donlin-Asp\, Ph.D.\nPostdoctoral Researcher\nDepartment of Synaptic Plasticity\nMax Planck Institute for Brain Research \n  \n  \n  \n  \nFlyer in PDF \nCo-Host: The Department of Molecular\, Cellular\, and Developmental Biology \nHybrid Seminar:\nIn-person: Biomedical Science Research Building (BSRB)\, ABC Seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_tZjYxppSQwaDVTYIuC0jkw \nKeywords: mRNA dynamics\, local protein synthesis\, neurons\, neuronal cell biology\, synaptic plasticity\, in vivo imaging \nIn-person event COVID guidelines
URL:https://rna.umich.edu/events/donlin-asp/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20211220T160000
DTEND;TZID=America/Detroit:20211220T170000
DTSTAMP:20260504T112159
CREATED:20210827T134635Z
LAST-MODIFIED:20211210T212954Z
UID:9277-1640016000-1640019600@rna.umich.edu
SUMMARY:RNA Faculty Candidate Seminar: Dr. Alisha 'Jonesy' Jones\, Institute of Structural Biology\, Helmholtz Zentrum Munich
DESCRIPTION:“Modulation of the MALT1 pre-mRNA structure by hnRNP proteins regulates T cell activation”\nDr. Alisha ‘Jonesy’ Jones\nPostdoctoral Researcher\nInstitute of Structural Biology\nHelmholtz Zentrum Munich \n  \n  \nFlyer in PDF  \nCo-Hosts: The Center for RNA Biomedicine\, Department of Biological Chemistry\, and the Program in Biophysics \nHybrid Seminar:\nIn-person: Biomedical Science Research Buliding (BSRB)\, ABC Seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_3yrQ47UuTKKuzigbe38Sww \nKeywords: pre-mRNA\, hnRNP\, NMR\, SHAPE\, structure \nAbstract: Alternative splicing is controlled by differential binding of trans-acting RNA binding proteins (RBPs) to cis-regulatory pre-mRNA elements. How pre-mRNA secondary structure affects recognition by RBPs and determines alternative exon usage is poorly understood. The MALT1 paracaspase is a key component of signaling pathways that mediate innate and adaptive immune responses. Alternative splicing of MALT1 exon7 is critical for controlling optimal T cell activation. Here\, we demonstrate that MALT1 pre-mRNA splicing depends on RNA structural elements that shield the splice sites of the alternatively spliced exon7. The RBPs hnRNP U and hnRNP L bind comparably and competitively to identical stem-loop RNA structures flanking the 5’ and 3’ splice sites of MALT1 exon7. While hnRNP U stabilizes RNA stem-loop conformations that maintain exon7 skipping\, hnRNP L destabilizes these RNA elements to facilitate recruitment of the essential splicing factor U2AF2 to promote exon7 inclusion. This work represents a paradigm for the control of splice site selection by differential RBP binding and modulation of pre-mRNA structure. \nIn-person event COVID guidelines
URL:https://rna.umich.edu/events/alisha-jonesy-jones/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220110T160000
DTEND;TZID=America/Detroit:20220110T170000
DTSTAMP:20260504T112159
CREATED:20211130T161429Z
LAST-MODIFIED:20220105T212127Z
UID:9805-1641830400-1641834000@rna.umich.edu
SUMMARY:RNA Faculty Candidate Seminar: Rachel Niederer\, Yale School of Medicine
DESCRIPTION:“Uncovering novel translational control elements within 5′ UTRs”\nRachel Niederer\, Ph.D.\nPostdoctoral Researcher\nYale School of Medicine \n  \nCo-Hosts: The Center for RNA Biomedicine\, Department of Biological Chemistry\, and the Department of Human Genetics \nHybrid Seminar:\nIn-person: Biomedical Science Research Buliding (BSRB)\, ABC Seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_qg4fyCUbQZyVu0oGrBLmWQ \nAbstract: Translational control of gene expression plays an essential role during development\, response to stress and a wide range of cellular processes. However\, the key mRNA features that distinguish efficiently translated from poorly translated mRNAs remain largely unknown. This talk will describe the development of direct analysis of ribosome targeting (DART) and its use both in discovering novel regulatory elements within 5′ untranslated regions (5′ UTRs) as well as revealing unexpected behaviors from features that were previously thought to be well understood. \nIn-person event COVID guidelines \nFlyer in PDF
URL:https://rna.umich.edu/events/rachel-niederer/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220131T160000
DTEND;TZID=America/Detroit:20220131T170000
DTSTAMP:20260504T112159
CREATED:20211130T164405Z
LAST-MODIFIED:20220104T163046Z
UID:9808-1643644800-1643648400@rna.umich.edu
SUMMARY:RNA Faculty Candidate Seminar: Jailson (Jay) Brito Querido\, MRC Laboratory of Molecular Biology
DESCRIPTION:“The scanning mechanism of mRNA translation initiation in humans”\nJailson (Jay) Brito Querido\, Ph.D.\nPostdoctoral Scientist\nMRC Laboratory of Molecular Biology\nCambridge\, UK \n  \n  \n  \nCo-Hosts: The Center for RNA Biomedicine\, Department of Biological Chemistry\, and the Program in Biophysics \nHybrid Seminar:\nIn-person: Biomedical Science Research Building (BSRB)\, ABC Seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_pcS-fWIdSS-hDnKzoRhXeg \nKeywords: mRNA\, translation\, ribosome\, helicase\nAbstract: Decoding the genetic information into protein is fundamental for all kingdoms of life. It requires precise mechanisms to transcribe the DNA into mRNA\, which then can be translated by the ribosome to produce proteins. Translation initiation of eukaryotic mRNAs is a dynamic process regulated by over a dozen protein eukaryotic initiation factors (eIFs). This process starts with the binding of eukaryotic initiation factors eIF1\, eIF1A\, eIF3\, eIF5\, and a ternary complex of eIF2–GTP–tRNAiMet (TC) to the 40S small ribosomal subunit\, forming the 43S preinitiation complex (43S PIC). Once assembled\, the 43S PIC is recruited to the 5′ untranslated region (UTR) of mRNA by the multifactor cap-binding complex eIF4F\, forming the 48S initiation complex (48S). The 48S then scans along the 5′ UTR mRNA to locate a start codon. The eIF4F binding site in the 48S and how mRNA is inserted into the mRNA channel in the 40S small ribosomal subunit remained unknown. To gain insights into the molecular mechanism underlining the assembly of the 48S\, we used cryo-electron microscopy to determine the structure of a reconstituted human 48S. The structure sheds light on the early events of translation initiation complex assembly\, including how eIF4F interacts with the 43S during the scanning process. \nIn-person COVID Events Policy
URL:https://rna.umich.edu/events/jay-brito-querido/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220214T160000
DTEND;TZID=America/Detroit:20220214T170000
DTSTAMP:20260504T112159
CREATED:20211130T173006Z
LAST-MODIFIED:20220204T174223Z
UID:9812-1644854400-1644858000@rna.umich.edu
SUMMARY:RNA Faculty Candidate Seminar: Margaret (Maggie) Rodgers\, Johns Hopkins University
DESCRIPTION:“Mechanisms of co-transcriptional ribonucleoprotein assembly”\nMargaret (Maggie) Rodgers\, Ph.D.\nPostdoctoral Researcher\nJohns Hopkins University \n  \n  \n  \n  \nCo-Hosts: The Center for RNA Biomedicine\, Department of Biological Chemistry\, and the Program in Biophysics \nHybrid Seminar:\nIn-person: Biomedical Science Research Buliding (BSRB)\, ABC Seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_Icqg8jRbQNGCBEFkj_u5Gw \nKeywords: RNA\, RNP\, ribosome assembly\, transcription\, single-molecule fluorescence \nSeminar flyer in PDF \nIn-person event COVID guidelines
URL:https://rna.umich.edu/events/margaret-maggie-rodgers/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220228T160000
DTEND;TZID=America/Detroit:20220228T170000
DTSTAMP:20260504T112159
CREATED:20220214T173408Z
LAST-MODIFIED:20220214T212905Z
UID:10113-1646064000-1646067600@rna.umich.edu
SUMMARY:Seminar: John Prensner\, MD\, PhD
DESCRIPTION:“Translating the cancer genome: dark matter proteins”\nJohn Prensner\, M.D.\, Ph.D.\nPhysician\, Dana-Farber/Boston Children’s Cancer and Blood Disorders Center\nInstructor of Pediatrics\, Harvard Medical School \n  \n  \nCo-Hosts: The Center for RNA Biomedicine\, Department of Computational Medicine & Bioinformatics\, and Department of Pediatric Oncology \nHybrid Seminar:\nIn-person: Biomedical Science Research Building (BSRB)\, ABC Seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_bC6oy6VZTLy3ke4iMS2sKQ \nKeywords: cancer\, ribosome profiling\, functional genomics\, gene discovery \nAbstract: Although genomic analyses predict many non-canonical open reading frames (ORFs) in the human genome\, it is unclear whether they encode biologically active proteins in diseases such as cancer. Here\, we have developed functional genomics platforms to systematically interrogate non-canonical ORFs identified in ribosome profiling data. Using CRISPR loss-of-function screens in numerous human cancer models\, we define the frequency with which ORFs contribute to cell essentiality phenotypes. We further constructed large-scale ORF plasmid libraries to assess their capacity to encode a protein and induce cancer cell transcriptional changes. We pursued focused investigation of several uncharacterized protein-coding loci\, defining roles for the lncRNA-ORF GREP1 in breast cancer and the ASNSD1 upstream ORF (uORF) in medulloblastoma. Lastly\, we have assembled a pathway to bring such ORF candidates into the mainstream of biological research via an international consortium of gene database stakeholders. Together\, this work establishes non-canonical ORFs as critical mediators of cancer cell biology\, suggests their potential promise as therapeutic targets in cancer\, and outlines a path forward for dissemination of these ORFs amongst the global research community. \nIn-person COVID Events Policy
URL:https://rna.umich.edu/events/john-prensner/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220321T150000
DTEND;TZID=America/Detroit:20220321T160000
DTSTAMP:20260504T112159
CREATED:20220314T142057Z
LAST-MODIFIED:20220314T183351Z
UID:10183-1647874800-1647878400@rna.umich.edu
SUMMARY:RNA Therapeutics Seminar\, Michelle Hastings\, Rosalind Franklin University
DESCRIPTION:Inaugural RNA Therapeutics Seminar\nMichelle Hastings\, Ph.D.\nProfessor\, Cell Biology and Anatomy; Director\, Center for Genetic Diseases\nRosalind Franklin University of Medicine and Science \n  \n  \n  \nThis is an internal U-M event:\nIn-person: Palmer Commons\, Forum Hall\nZoom: https://umich.zoom.us/webinar/register/WN_mUj40sudTwmI6hXANnlJEg \nKeywords: pre-mRNA splicing\, Antisense oligonucleotides\, Usher syndrome\, Batten Disease\, lysosomal storage diseases \nSeminar flyer in PDF \nIn-person COVID Events Policy
URL:https://rna.umich.edu/events/rna-therapeutics-seminar-michelle-hastings/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220509T160000
DTEND;TZID=America/Detroit:20220509T170000
DTSTAMP:20260504T112159
CREATED:20211216T202325Z
LAST-MODIFIED:20220502T191433Z
UID:9963-1652112000-1652115600@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Sika Zheng\, UC Riverside\, School of Medicine
DESCRIPTION:“Unexpected determinants of neuronal identity and properties: the curious cases of PTBP1\, PTBP2\, and neuronal splicing”\nSika Zheng\, Ph.D. \nAssociate Professor\, Director of Center for RNA Biology and Medicine\nUC Riverside\, School of Medicine \n  \nFlyer in PDF \n  \nVirtual Seminar\nZoom: https://umich.zoom.us/webinar/register/WN_dltbxWdHQ5KrC3rTl4hqLQ \nAbstract:\nAlternative splicing is the major contributor to transcriptome diversity\, but splicing is noisy and to what extend alternative splicing regulation is indispensable for biolgical processes has been controversial. Our studies have revealed the regulation and function of neural-specific splicing in shaping neuronal identity and estalishing neurons’ two unique attributes: 1. Axonogenesis (Only neurons but no other cell types have one and single axon); 2. Neuronal longevity (Neurons are the most long-lived cell types). We show that obtaining these neuronal features is coordinated by RNA binding proteins PTBP1 and PTBP2\, while PTBP1 was suggested by others to be a reprogramming factor of neuronal fate. I will discuss the regulatory mechanism of neural specific splicing underlying neurogensis and maturation. \nReferences:\nZhang M\, Ergin V\, Lin L\, Stork C\, Chen L\, Zheng S. Neuron. 2019 Feb 20;101(4):690-706.e10.\nErgin V\, Zheng S. J Mol Biol. 2020 Jun 26;432(14):4154-4166.\nZheng S. Wiley Interdiscip Rev RNA. 2020 Jul;11(4):e1585.\nLin L\, Zhang M\, Stoilov P\, Chen L\, Zheng S. Neuron. 2020 Sep 23;107(6):1180-1196.e8.\nVuong J\, Ergin V\, Zheng S. Nature Communications (accepted)
URL:https://rna.umich.edu/events/sika-zheng/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220516T160000
DTEND;TZID=America/Detroit:20220516T170000
DTSTAMP:20260504T112159
CREATED:20220218T163352Z
LAST-MODIFIED:20220506T161447Z
UID:10130-1652716800-1652720400@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Daniel O’Reilly
DESCRIPTION:“An Academic Approach to Oligonucleotide Therapeutics”\nDaniel O’Reilly Ph.D.\, MRSC\nPost-Doctoral Associate\nKhvorova Lab\nRNA Therapeutics Institute\nUniversity of Massachusetts Medical School \nFlyer in PDF \n  \nHYBRID SEMINAR:\nIn-person: BSRC\, ABC seminar rooms\nZoom: https://umich.zoom.us/webinar/register/WN_dM1a1aKVTM2KfwiieutOWg \nKeywords: Oligonucleotides\, Chemical Modifications\, RNA\, Huntington’s Disease \nAbstract: Nucleic acids (NA) are becoming the third major pillar of therapeutic modalities on par with small molecules and biologics. The diversity of NA molecular mechanisms\, ranging from vaccines\, antisense\, short interfering RNA (siRNAs)\, and guide RNA for CRISPR gene editing systems\, enable impact on most aspects of cellular biology and thus human medicine. The foundation behind the recent oligonucleotides’ clinical success is fundamental chemical innovations in RNA stability\, delivery\, and synthesis.\nOligonucleotides are informational drugs; thus\, if chemical architectures supporting safe and efficient delivery to the tissue of interest are achieved\, they can be easily reprogrammed to modulate any gene expression on demand\, creating an opportunity for academic institutions to drive therapeutic innovation. However\, the process is limited by access to oligonucleotide chemistry and synthetic expertise.\nIn the first half of the talk\, I will share the experience of building and running Nucleic Acid Chemistry Center in a context of a large academic institution. The NACC provides access to therapeutic quality screening leads and large manufacturing of preclinical compounds for the academic community. The impact of the NACC and chemical innovation will be discussed in the context of two significant projects. First\, I will discuss the systematic structure-activity relationship study of chemical modifications to modulate RISC loading and cleavage. Screening 1200 siRNA variants allow for defining the chemical and thermodynamic rules for RISC assembly.
URL:https://rna.umich.edu/events/daniel-oreilly/
CATEGORIES:Seminar
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=America/Detroit:20220912T160000
DTEND;TZID=America/Detroit:20220912T170000
DTSTAMP:20260504T112159
CREATED:20220826T123641Z
LAST-MODIFIED:20220829T141846Z
UID:10539-1662998400-1663002000@rna.umich.edu
SUMMARY:RNA Innovation Seminar: Zhipeng Lu\, USC
DESCRIPTION:“RNA Structures\, Interactions and Modifications”\nZhipeng Lu (鲁志鹏)\, Ph.D.\nAssistant Professor\nPharmacology and Pharmaceutical Sciences\nUniversity of Southern California \n  \nFlyer in PDF \nIn-person: BSRB\, ABC seminar rooms / hybrid link \nAbstract: RNA in living cells are in constant motion\, form dynamic structures\, and interact with many molecules\, including other RNAs. Direct determination of RNA structures and interactions in vivo is essential to understanding their functions\, but has been challenging in the past. We developed a number of novel chemical and computational tools to capture the 2D and 3D RNA structurome and interactome in cells\, providing a comprehensive view of RNA conformations that underlie their roles in gene regulation and human diseases. Applications of these methods revealed new mechanisms in lncRNA functions\, RNA modifications and splicing regulation.
URL:https://rna.umich.edu/events/zhipeng-lu/
CATEGORIES:Seminar
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END:VCALENDAR