Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/29053
Title: Structural investigations of the RNA-binding properties of STAR proteins
Authors: Feracci, Mikael
Foot, Jaelle
Dominguez, Cyril
First Published: 1-Aug-2014
Publisher: Portland Press
Citation: Biochemical Society Transactions, 2014, 42 (4), pp. 1141-1146
Abstract: STAR (signal transduction and activation of RNA) proteins are a family of RNA-binding proteins that regulate post-transcriptional gene regulation events at various levels, such as pre-mRNA alternative splicing, RNA export, translation and stability. Most of these proteins are regulated by signalling pathways through post-translational modifications, such as phosphorylation and arginine methylation. These proteins share a highly conserved RNA-binding domain, denoted STAR domain. Structural investigations of this STAR domain in complex with RNA have highlighted how a subset of STAR proteins specifically recognizes its RNA targets. The present review focuses on the structural basis of RNA recognition by this family of proteins.
DOI Link: 10.1042/BST20140081
ISSN: 0300-5127
eISSN: 1470-8752
Links: http://www.biochemsoctrans.org/content/42/4/1141
http://hdl.handle.net/2381/29053
Version: Post-print
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © The Authors Journal compilation © 2014 Biochemical Society. Deposited with reference to the publisher’s archiving policy available on the SHERPA/RoMEO website.
Description: The final version of record is available at http://www.biochemsoctrans.org/content/42/4/1141
Appears in Collections:Published Articles, Dept. of Biochemistry

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