@article{daf38922b4714500b7d7f4213aefd3f4,
title = "Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68",
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.",
author = "Mikael Feracci and Foot, {Jaelle N.} and Grellscheid, {Sushma N.} and Marina Danilenko and Ralf Stehle and Oksana Gonchar and Kang, {Hyun Seo} and Caroline Dalgliesh and Meyer, {N. Helge} and Yilei Liu and Albert Lahat and Michael Sattler and Eperon, {Ian C.} and Elliott, {David J.} and Cyril Dominguez",
note = "Funding Information: We thank J. Schwabe, L. Fairall, P. Watson, P. Moody and the staff at beamlines I03, I04 and I04-1 at the Diamond Light Source for assistance with X-ray crystallization, data collection and structure determination; the facility of the SFB1035 at the Chemistry Department, Technische Universit{\"a}t M{\"u}nchen for SAXS measurements; X. Yang (PROTEX) for the cloning facility; F. Muskett for NMR support; K. Sidhu for IT support; C. Weldon, and S. Jayne for discussion. This work was supported by a Medical Research Council Career Development Award (MRC CDA) to C.Do. (G1000526), a College of Medicine, Biological Sciences and Psychology, University of Leicester, studentship to J.N.F., a BBSRC grant to D.J.E. (BB/K018957/1) and the Deutsche Forschungsgemeinschaft DFG (grants SFB1035 and GRK1721) to M.S. Funding Information: We thank J. Schwabe, L. Fairall, P. Watson, P. Moody and the staff at beamlines I03, I04 and I04-1 at the Diamond Light Source for assistance with X-ray crystallization, data collection and structure determination; the facility of the SFB1035 at the Chemistry Department, Technische Universit{\"a}t M{\"u}nchen for SAXS measurements; X. Yang (PROTEX) for the cloning facility; F. Muskett for NMR support; K. Sidhu for IT support; C. Weldon, and S. Jayne for discussion. This work was supported by a Medical Research Council Career Development Award (MRC CDA) to C. Do. (G1000526), a College of Medicine, Biological Sciences and Psychology, University of Leicester, studentship to J.N.F., a BBSRC grant to D.J.E. (BB/K018957/1) and the Deutsche Forschungsgemeinschaft DFG (grants SFB1035 and GRK1721) to M.S.",
year = "2016",
month = jan,
day = "13",
doi = "10.1038/ncomms10355",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Research",
}