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Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.

Feracci, Mikael and Foot, Jaelle N. and Grellscheid, Sushma N. and Danilenko, Marina and Stehle, Ralf and Gonchar, Oksana and Kang, Hyun-Seo and Dalgliesh, Caroline and Meyer, N. Helge and Liu, Yilei and Lahat, Albert and Sattler, Michael and Eperon, Ian C. and Elliott, David J. and Dominguez, Cyril (2016) 'Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.', Nature communications., 7 . p. 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.

Item Type:Article
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Status:Peer-reviewed
Publisher Web site:https://doi.org/10.1038/ncomms10355
Publisher statement:This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Date accepted:01 December 2015
Date deposited:13 October 2017
Date of first online publication:13 January 2016
Date first made open access:13 October 2017

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