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dc.contributor.authorVindry, Carolineen
dc.contributor.authorWeil, Dominiqueen
dc.contributor.authorStandart, Nancyen
dc.date.accessioned2019-05-10T23:30:53Z
dc.date.available2019-05-10T23:30:53Z
dc.date.issued2019-11en
dc.identifier.issn1757-7004
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/292687
dc.description.abstractPost-transcriptional regulation of gene expression is largely achieved at the level of splicing in the nucleus, and translation and mRNA decay in the cytosol. While the regulation may be global, through the direct inhibition of central factors, such as the spliceosome, translation initiation factors and mRNA decay enzymes, in many instances transcripts bearing specific sequences or particular features are regulated by RNA-binding factors which mobilize or impede recruitment of these machineries. This review focuses on the Pat1 family of RNA-binding proteins, conserved from yeast to man, that enhance the removal of the 5’ cap by the decapping enzyme Dcp1/2, leading to mRNA decay and also have roles in translational repression. Like Dcp1/2, other decapping co-activators including DDX6 and Edc3, and translational repressor proteins, Pat1 proteins are enriched in cytoplasmic P-bodies, which have a principal role in mRNA storage. They also concentrate in nuclear Cajal-bodies and splicing speckles and in man, impact splice site choice in some pre-mRNAs. Pivotal to these functions is the association of Pat1 proteins with distinct heptameric Lsm complexes: the cytosolic Pat1/Lsm1-7 complex mediates mRNA decay and the nuclear Pat1/Lsm2-8 complex alternative splicing. This dual role of human Pat1b illustrates the power of paralogous complexes to impact distinct processes in separate compartments. The review highlights our recent findings that Pat1b mediates the decay of AU-rich mRNAs, which are particularly enriched in P-bodies, unlike the decapping activator DDX6, which acts on GC-rich mRNAs, that tend to be excluded from P-bodies, and discuss the implications for mRNA decay pathways.
dc.description.sponsorshipThis work was supported by the BBSRC, Newton Trust and Foundation Wiener – Anspach (C.V.) to N.S.’s laboratory, and the Association pour la Recherche sur le Cancer and the Agence Nationale pour la Recherche contract ANR-14-CE09-0013-01 to D.W.’s laboratory.
dc.format.mediumPrint-Electronicen
dc.languageengen
dc.rightsAll rights reserved
dc.rights.uri
dc.subjectHumansen
dc.subjectRNA-Binding Proteinsen
dc.subjectRNA, Messengeren
dc.titlePat1 RNA-binding proteins: Multitasking shuttling proteins.en
dc.typeArticle
prism.issueIdentifier6en
prism.publicationDate2019en
prism.publicationNameWiley interdisciplinary reviews. RNAen
prism.startingPagee1557
prism.volume10en
dc.identifier.doi10.17863/CAM.39840
dcterms.dateAccepted2019-05-07en
rioxxterms.versionofrecord10.1002/wrna.1557en
rioxxterms.versionAM
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2019-11en
dc.contributor.orcidVindry, Caroline [0000-0002-2038-0288]
dc.contributor.orcidWeil, Dominique [0000-0001-7630-1772]
dc.contributor.orcidStandart, Nancy [0000-0001-5963-6255]
dc.identifier.eissn1757-7012
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idBBSRC (BB/J00779X/1)
pubs.funder-project-idIsaac Newton Trust (1507(d))
cam.orpheus.successThu Jan 30 10:45:36 GMT 2020 - Embargo updated*
rioxxterms.freetoread.startdate2020-11-30


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