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RNPS 1 is modulated by ubiquitin‐specific protease 4
Author(s) -
Kwon SeulKi,
Kim EunHea,
Baek KwangHyun
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12531
Subject(s) - spliceosome , rna splicing , alternative splicing , ubiquitin , serine protease , messenger rna , protein splicing , protease , biology , microbiology and biotechnology , biochemistry , rna , chemistry , enzyme , gene
RNA ‐binding protein with serine‐rich domain 1 ( RNPS 1) is a component of pre‐splicing and post‐splicing multiprotein complexes, which activates constitutive and alternative splicing. RNPS 1 participates in the formation of the spliceosome and activates the pre‐ mRNA splicing process. In the present study, we found that ubiquitin‐specific protease 4 ( USP 4) is a binding partner of RNPS 1. Although RNPS 1 is polyubiquitinated by both K48‐ and K63‐linkages, USP 4 exclusively deubiquitinates K63‐linked polyubiquitin chains of RNPS 1. We also demonstrate that the catalytic activity of USP 4 on ubiquitinated RNPS 1 is elevated by squamous cell carcinoma antigen recognized by T cells 3 (Sart3).