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

Lookup NU author(s): Dr Sushma Grellscheid, Dr Marina Danilenko, Caroline Dalgliesh, Yilei Liu, Professor David Elliott



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


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.

Publication metadata

Author(s): Feracci M, Foot JN, Grellscheid SN, Danilenko M, Stehle R, Gonchar O, Kang HS, Dalgliesh C, Meyer NH, Liu YL, Lahat A, Sattler M, Eperon IC, Elliott DJ, Dominguez C

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2016

Volume: 7

Online publication date: 13/01/2016

Acceptance date: 01/12/2015

Date deposited: 24/03/2016

ISSN (electronic): 2041-1723

Publisher: Nature Publishing Group


DOI: 10.1038/ncomms10355


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Funder referenceFunder name
College of Medicine, Biological Sciences and Psychology, University of Leicester
G1000526Medical Research Council Career Development Award (MRC CDA)
GRK1721Deutsche Forschungsgemeinschaft DFG
SFB1035Deutsche Forschungsgemeinschaft DFG