Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif
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- 作者：Pedro Serrano1 ; &dagger ; ; Brandon E. Aubol2 ; &dagger ; ; Malik M. Keshwani2 ; Stefano Forli2 ; Chen-Ting Ma2 ; Samit K. Dutta1 ; 4 ; Michael Geralt1 ; Kurt Wü ; thrich1 ; 3 ; Joseph A. Adams2 ; j2adams@ucsd.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：RRM ; RNA recognition motif ; RS domain ; domain rich in arginine&ndash ; serine dipeptide repeats ; SR protein ; splicing factor containing arginine&ndash ; serine dipeptide repeats ; SRPK1 ; serine&ndash ; arginine-specific protein kinase 1 ; SRSF1 ; SR protein splicing factor 1 (aka ASF/SF2) ; NOESY ; NOE spectroscopy ; HSQC ; heteronuclear single quantum coherence
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：5 June 2016
- 年：2016
- 卷：428
- 期：11
- 页码：2430-2445
- 全文大小：2674 K
文摘
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SRPK1 catalyzes multisite phosphorylation of SRSF1 using a directional mechanism.
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Several charged residues in RRM2 interact with RS domain in SRSF1.
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RRM2–RS domain interactions control directional phosphorylation.
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Directional phosphorylation regulates subcellular localization of SRSF1.
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Phosphorylation mechanism is tied to biological function of an SR protein.