Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
Full metadata record
DC FieldValueLanguage
dc.contributor.authorAthanasopoulos, V.-
dc.contributor.authorBarker, A.-
dc.contributor.authorYu, D.-
dc.contributor.authorTan, A.-
dc.contributor.authorSrivastava, M.-
dc.contributor.authorContreras, N.-
dc.contributor.authorWang, J.-
dc.contributor.authorLam, K.-
dc.contributor.authorBrown, S.-
dc.contributor.authorGoodnow, C.-
dc.contributor.authorDixon, N.-
dc.contributor.authorLeedman, P.-
dc.contributor.authorSaint, R.-
dc.contributor.authorVinuesa, C.-
dc.identifier.citationThe Federation of European Biochemical Societies (FEBS) Journal, 2010; 277(9):2109-2127-
dc.description.abstractRoquin is an E3 ubiquitin ligase with a poorly understood but essential role in preventing T-cell-mediated autoimmune disease and in microRNA-mediated repression of inducible costimulator (Icos) mRNA. Roquin and its mammalian paralogue membrane-associated nucleic acid binding protein (MNAB) define a protein family distinguished by an ∼ 200 amino acid domain of unknown function, ROQ, that is highly conserved from mammals to invertebrates and is flanked by a RING-1 zinc finger and a CCCH zinc finger. Here we show that human, Drosophila and Caenorhabditis elegans Roquin and human MNAB localize to the cytoplasm and upon stress are concentrated in stress granules, where stalled mRNA translation complexes are stored. The ROQ domain is necessary and sufficient for localization to arsenite-induced stress granules and to induce these structures upon overexpression, and is required to trigger Icos mRNA decay. Gel-shift, SPR and footprinting studies show that an N-terminal fragment centred on the ROQ domain binds RNA from the Icos 3′-untranslated region comprising the minimal sequence for Roquin-mediated repression, adjacent to the miR-101 sequence complementarity. These findings identify Roquin as an RNA-binding protein and establish a specific function for the ROQ protein domain in mRNA homeostasis.-
dc.description.statementofresponsibilityVicki Athanasopoulos, Andrew Barker, Di Yu, Andy H-M. Tan, Monika Srivastava, Nelida Contreras, Jianbin Wang, Kong-Peng Lam, Simon H. J. Brown, Christopher C. Goodnow, Nicholas E. Dixon, Peter J. Leedman, Robert Saint, and Carola G. Vinuesa-
dc.publisherBlackwell Publishing Ltd-
dc.rights© 2010 The Authors-
dc.subjectmembrane-associated nucleic acid binding protein-
dc.subjectstress granules-
dc.titleThe ROQUIN family of proteins localizes to stress granules via the ROQ domain and binds target mRNAs-
dc.typeJournal article-
dc.contributor.organisationOffice of the Deputy Vice-Chancellor and Vice-President (Research)-
Appears in Collections:Aurora harvest 4
Molecular and Biomedical Science publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.