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Feracci, M.* ; Foot, J.N.* ; Grellscheid, S.N.* ; Danilenko, M.* ; Stehle, R.* ; Gonchar, O.* ; Kang, H.-S. ; Dalgliesh, C.* ; Meyer, N.H. ; Liu, Y.* ; Lahat, A.* ; Sattler, M. ; Eperon, I.C.* ; Elliott, D.J.* ; Dominguez, C.*

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

Nat. Commun. 7:10355 (2016)
Verlagsversion DOI
Open Access Gold
Creative Commons Lizenzvertrag
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Binding Protein; Messenger-rna; Src Substrate; Rev Function; Cell Lines; Kh-domain; Mitosis; Gld-1; Specificity; Homodimerization
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Zeitschrift Nature Communications
Quellenangaben Band: 7, Heft: , Seiten: , Artikelnummer: 10355 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus Peer reviewed