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

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

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Authors

Mikael Feracci

Jaelle N. Foot

Marina Danilenko

Ralf Stehle

Oksana Gonchar

Hyun-Seo Kang

Caroline Dalgliesh

N. Helge Meyer

Yilei Liu

Albert Lahat

Michael Sattler

Ian C. Eperon

David J. Elliott

Cyril Dominguez



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.

Citation

Feracci, M., Foot, J. N., Grellscheid, S. N., Danilenko, M., Stehle, R., Gonchar, O., …Dominguez, C. (2016). Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68. Nature Communications, 7, Article 10355. https://doi.org/10.1038/ncomms10355

Journal Article Type Article
Acceptance Date Dec 1, 2015
Online Publication Date Jan 13, 2016
Publication Date Jan 13, 2016
Deposit Date Aug 25, 2017
Publicly Available Date Mar 29, 2024
Journal Nature Communications
Publisher Nature Research
Peer Reviewed Peer Reviewed
Volume 7
Article Number 10355
DOI https://doi.org/10.1038/ncomms10355

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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/





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