气候变化领域集成服务门户(CCPortal): CLK1 reorganizes the splicing factor U1-70K for early spliceosomal protein assembly

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DOI	10.1073/pnas.2018251118
	CLK1 reorganizes the splicing factor U1-70K for early spliceosomal protein assembly
	Aubol B.E.; Wozniak J.M.; Fattet L.; Gonzalez D.J.; Adams J.A.
发表日期	2021
ISSN	00278424
卷号	118 期号:14
英文摘要	Early spliceosome assembly requires phosphorylation of U1-70K, a constituent of the U1 small nuclear ribonucleoprotein (snRNP), but it is unclear which sites are phosphorylated, and by what enzyme, and how such modification regulates function. By profiling the proteome, we found that the Cdc2-like kinase 1 (CLK1) phosphorylates Ser-226 in the C terminus of U1-70K. This releases U1-70K from subnuclear granules facilitating interaction with U1 snRNP and the serine-arginine (SR) protein SRSF1, critical steps in establishing the 5' splice site. CLK1 breaks contacts between the C terminus and the RNA recognition motif (RRM) in U1-70K releasing the RRM to bind SRSF1. This reorganization also permits stable interactions between U1-70K and several proteins associated with U1 snRNP. Nuclear induction of the SR protein kinase 1 (SRPK1) facilitates CLK1 dissociation from U1-70K, recycling the kinase for catalysis. These studies demonstrate that CLK1 plays a vital, signaldependent role in early spliceosomal protein assembly by contouring U1-70K for protein-protein multitasking. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Kinase; Phosphorylation; Regulation; Splicing
语种	英语
scopus关键词	cyclin dependent kinase 1; protein SRPK1; protein SRSF1; protein U1 70K; serine arginine rich protein; small nuclear ribonucleoprotein; unclassified drug; Article; carboxy terminal sequence; catalysis; confocal microscopy; controlled study; cytolysis; immunoprecipitation; liquid chromatography-mass spectrometry; priority journal; protein analysis; protein assembly; protein expression; protein function; protein phosphorylation; protein protein interaction; protein purification; protein RNA binding; protein secretion; protein targeting; proteomics; RNA recognition motif; spliceosome; TMT labeling
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/179954
作者单位	Department of Pharmacology, University of California San Diego, San diego, CA 92093, United States; Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San diego, CA 92093, United States; Collaborative Center for Multiplexing Proteomics, University of California San Diego, San diego, CA 92093, United States
推荐引用方式 GB/T 7714	Aubol B.E.,Wozniak J.M.,Fattet L.,et al. CLK1 reorganizes the splicing factor U1-70K for early spliceosomal protein assembly[J],2021,118(14).
APA	Aubol B.E.,Wozniak J.M.,Fattet L.,Gonzalez D.J.,&Adams J.A..(2021).CLK1 reorganizes the splicing factor U1-70K for early spliceosomal protein assembly.Proceedings of the National Academy of Sciences of the United States of America,118(14).
MLA	Aubol B.E.,et al."CLK1 reorganizes the splicing factor U1-70K for early spliceosomal protein assembly".Proceedings of the National Academy of Sciences of the United States of America 118.14(2021).