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dc.contributor.authorHuang, Yi-Shuian
dc.contributor.authorKan, Ming-Chung
dc.contributor.authorLin, Chien-Ling
dc.contributor.authorRichter, Joel D.
dc.date2022-08-11T08:08:59.000
dc.date.accessioned2022-08-23T16:14:36Z
dc.date.available2022-08-23T16:14:36Z
dc.date.issued2006-10-07
dc.date.submitted2008-10-09
dc.identifier.citationEMBO J. 2006 Oct 18;25(20):4865-76. Epub 2006 Oct 5. <a href="http://dx.doi.org/10.1038/sj.emboj.7601322 ">Link to article on publisher's site</a>
dc.identifier.issn0261-4189 (Print)
dc.identifier.doi10.1038/sj.emboj.7601322
dc.identifier.pmid17024188
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33900
dc.description.abstractCPEB is a sequence-specific RNA-binding protein that promotes polyadenylation-induced translation in oocytes and neurons. Vertebrates contain three additional genes that encode CPEB-like proteins, all of which are expressed in the brain. Here, we use SELEX, RNA structure probing, and RNA footprinting to show that CPEB and the CPEB-like proteins interact with different RNA sequences and thus constitute different classes of RNA-binding proteins. In transfected neurons, CPEB3 represses the translation of a reporter RNA in tethered function assays; in response to NMDA receptor activation, translation is stimulated. In contrast to CPEB, CPEB3-mediated translation is unlikely to involve cytoplasmic polyadenylation, as it requires neither the cis-acting AAUAAA nor the trans-acting cleavage and polyadenylation specificity factor, both of which are necessary for CPEB-induced polyadenylation. One target of CPEB3-mediated translation is GluR2 mRNA; not only does CPEB3 bind this RNA in vitro and in vivo, but an RNAi knockdown of CPEB3 in neurons results in elevated levels of GluR2 protein. These results indicate that CPEB3 is a sequence-specific translational regulatory protein.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17024188&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1038/sj.emboj.7601322
dc.subject3' Untranslated Regions; Animals; Cell Line; Male; Mice; Neurons; Polyadenylation; Protein Binding; *Protein Biosynthesis; RNA, Messenger; RNA-Binding Proteins; Rats; Receptors, AMPA; Transfection; Xenopus
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleCPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and translational control of AMPA receptor GluR2 mRNA
dc.typeJournal Article
dc.source.journaltitleThe EMBO journal
dc.source.volume25
dc.source.issue20
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/555
dc.identifier.contextkey646740
html.description.abstract<p>CPEB is a sequence-specific RNA-binding protein that promotes polyadenylation-induced translation in oocytes and neurons. Vertebrates contain three additional genes that encode CPEB-like proteins, all of which are expressed in the brain. Here, we use SELEX, RNA structure probing, and RNA footprinting to show that CPEB and the CPEB-like proteins interact with different RNA sequences and thus constitute different classes of RNA-binding proteins. In transfected neurons, CPEB3 represses the translation of a reporter RNA in tethered function assays; in response to NMDA receptor activation, translation is stimulated. In contrast to CPEB, CPEB3-mediated translation is unlikely to involve cytoplasmic polyadenylation, as it requires neither the cis-acting AAUAAA nor the trans-acting cleavage and polyadenylation specificity factor, both of which are necessary for CPEB-induced polyadenylation. One target of CPEB3-mediated translation is GluR2 mRNA; not only does CPEB3 bind this RNA in vitro and in vivo, but an RNAi knockdown of CPEB3 in neurons results in elevated levels of GluR2 protein. These results indicate that CPEB3 is a sequence-specific translational regulatory protein.</p>
dc.identifier.submissionpathgsbs_sp/555
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages4865-76


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