Staufen: from embryo polarity to cellular stress and neurodegeneration.
Identifieur interne : 000592 ( PubMed/Corpus ); précédent : 000591; suivant : 000593Staufen: from embryo polarity to cellular stress and neurodegeneration.
Auteurs : Leandro Julian Martinez Tosar ; Maria Gabriela Thomas ; Maria Veronica Baez ; Irene Ibanez ; Ariel Chernomoretz ; Graciela Lidia BoccaccioSource :
- Frontiers in bioscience (Scholar edition) [ 1945-0524 ] ; 2012.
English descriptors
- KwdEn :
- Animals, Humans, RNA (genetics), RNA (metabolism), RNA Stability, RNA Transport, RNA, Messenger (genetics), RNA, Messenger (metabolism), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), RNA-Binding Proteins (physiology), Ribonucleoproteins (genetics), Ribonucleoproteins (metabolism).
- MESH :
- chemical , genetics : RNA, RNA, Messenger, RNA-Binding Proteins, Ribonucleoproteins.
- chemical , metabolism : RNA, RNA, Messenger, RNA-Binding Proteins, Ribonucleoproteins.
- chemical , physiology : RNA-Binding Proteins.
- Animals, Humans, RNA Stability, RNA Transport.
Abstract
Staufen is a double-stranded RNA-binding protein that forms RNA granules by RNA-dependent and -independent interactions. Staufen was initially described in Drosophila as a key molecule for targeting maternal mRNAs. In vertebrates, two highly similar paralogs with several splicing variants mediate mRNA transport, thus affecting neuron plasticity, learning and memory. Staufen also regulates translation and mRNA decay. In recent years, Staufen was shown to be an important regulatory component of stress granules (SGs), which are large aggregates of silenced mRNPs specifically induced upon acute cellular stress. SGs contribute to cell survival by reprogramming translation and inhibiting pro-apoptotic pathways, and Staufen appears to negatively modulate SG formation by several mechanisms. More recently, mammalian Staufen was found in RNA granules and pathological cytoplasmic aggregates related to SGs containing huntingtin, TDP43, FUS/TLS or FMRP. In addition, Staufen binds CUG repeats present in mutant RNAs causative of degenerative conditions, thus ameliorating disease. Finally, Staufen affects HIV and influenza infection at several levels. Collectively, these observations unveil important roles for Staufen-mediated post-transcriptional regulation in a growing number of human diseases.
DOI: 10.2741/277
PubMed: 22202069
Links to Exploration step
pubmed:22202069Le document en format XML
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Staufen was initially described in Drosophila as a key molecule for targeting maternal mRNAs. In vertebrates, two highly similar paralogs with several splicing variants mediate mRNA transport, thus affecting neuron plasticity, learning and memory. Staufen also regulates translation and mRNA decay. In recent years, Staufen was shown to be an important regulatory component of stress granules (SGs), which are large aggregates of silenced mRNPs specifically induced upon acute cellular stress. SGs contribute to cell survival by reprogramming translation and inhibiting pro-apoptotic pathways, and Staufen appears to negatively modulate SG formation by several mechanisms. More recently, mammalian Staufen was found in RNA granules and pathological cytoplasmic aggregates related to SGs containing huntingtin, TDP43, FUS/TLS or FMRP. In addition, Staufen binds CUG repeats present in mutant RNAs causative of degenerative conditions, thus ameliorating disease. Finally, Staufen affects HIV and influenza infection at several levels. Collectively, these observations unveil important roles for Staufen-mediated post-transcriptional regulation in a growing number of human diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22202069</PMID><DateCompleted><Year>2013</Year><Month>08</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>12</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1945-0524</ISSN><JournalIssue CitedMedium="Internet"><Volume>4</Volume><PubDate><Year>2012</Year><Month>Jan</Month><Day>01</Day></PubDate></JournalIssue><Title>Frontiers in bioscience (Scholar edition)</Title><ISOAbbreviation>Front Biosci (Schol Ed)</ISOAbbreviation></Journal><ArticleTitle>Staufen: from embryo polarity to cellular stress and neurodegeneration.</ArticleTitle><Pagination><MedlinePgn>432-52</MedlinePgn></Pagination><Abstract><AbstractText>Staufen is a double-stranded RNA-binding protein that forms RNA granules by RNA-dependent and -independent interactions. Staufen was initially described in Drosophila as a key molecule for targeting maternal mRNAs. In vertebrates, two highly similar paralogs with several splicing variants mediate mRNA transport, thus affecting neuron plasticity, learning and memory. Staufen also regulates translation and mRNA decay. In recent years, Staufen was shown to be an important regulatory component of stress granules (SGs), which are large aggregates of silenced mRNPs specifically induced upon acute cellular stress. SGs contribute to cell survival by reprogramming translation and inhibiting pro-apoptotic pathways, and Staufen appears to negatively modulate SG formation by several mechanisms. More recently, mammalian Staufen was found in RNA granules and pathological cytoplasmic aggregates related to SGs containing huntingtin, TDP43, FUS/TLS or FMRP. In addition, Staufen binds CUG repeats present in mutant RNAs causative of degenerative conditions, thus ameliorating disease. Finally, Staufen affects HIV and influenza infection at several levels. Collectively, these observations unveil important roles for Staufen-mediated post-transcriptional regulation in a growing number of human diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tosar</LastName><ForeName>Leandro Julian Martinez</ForeName><Initials>LJ</Initials><AffiliationInfo><Affiliation>Facultad de Ciencias Exactas y Naturales, University of Buenos Aires, Buenos Aires, Argentina.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thomas</LastName><ForeName>Maria Gabriela</ForeName><Initials>MG</Initials></Author><Author ValidYN="Y"><LastName>Baez</LastName><ForeName>Maria Veronica</ForeName><Initials>MV</Initials></Author><Author ValidYN="Y"><LastName>Ibanez</LastName><ForeName>Irene</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Chernomoretz</LastName><ForeName>Ariel</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Boccaccio</LastName><ForeName>Graciela Lidia</ForeName><Initials>GL</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1R03 TW 06037-01A1</GrantID><Acronym>TW</Acronym><Agency>FIC NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>01</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Front Biosci (Schol Ed)</MedlineTA><NlmUniqueID>101485241</NlmUniqueID><ISSNLinking>1945-0516</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012261">Ribonucleoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C026452">messenger ribonucleoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020871" MajorTopicYN="N">RNA Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D034443" MajorTopicYN="N">RNA Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012261" MajorTopicYN="N">Ribonucleoproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>12</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>12</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22202069</ArticleId><ArticleId IdType="pii">277</ArticleId><ArticleId IdType="doi">10.2741/277</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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