Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/37023
Title: Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68
Authors: Feracci, Mikael
Foot, Jaelle N.
Grellscheid, Sushma N.
Danilenko, Marina
Stehle, Ralf
Gonchar, Oksana
Kang, Hyun-Seo
Dalgliesh, Caroline
Meyer, N. Helge
Liu, Yilei
Lahat, Albert
Sattler, Michael
Eperon, Ian C.
Elliott, David J.
Dominguez, Cyril
First Published: 13-Jan-2016
Publisher: Nature Publishing Group
Citation: Nature Communications, 2016, 7:10355
Abstract: Sam68 and T-STAR are members of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins. T-STAR is a tissue-specific paralogue that regulates the alternative splicing of neuronal pre-mRNAs. STAR proteins differ from most splicing factors, in that they contain a single RNA-binding domain. Their specificity of RNA recognition is thought to arise from their property to homodimerize, but how dimerization influences their function remains unknown. Here, we establish at atomic resolution how T-STAR and Sam68 bind to RNA, revealing an unexpected mode of dimerization different from other members of the STAR family. We further demonstrate that this unique dimerization interface is crucial for their biological activity in splicing regulation, and suggest that the increased RNA affinity through dimer formation is a crucial parameter enabling these proteins to select their functional targets within the transcriptome.
DOI Link: 10.1038/ncomms10355
eISSN: 2041-1723
Links: http://www.nature.com/ncomms/2016/160113/ncomms10355/full/ncomms10355.html
http://hdl.handle.net/2381/37023
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2016. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0/ ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Biology

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