title: RNPS1 is modulated by ubiquitin-specific protease 4.
abstract: RNA-binding protein with serine-rich domain 1 (RNPS1) is a component of pre-splicing and post-splicing multiprotein complexes, which activates constitutive and alternative splicing. RNPS1 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 (USP4) is a binding partner of RNPS1. Although RNPS1 is polyubiquitinated by both K48- and K63-linkages, USP4 exclusively deubiquitinates K63-linked polyubiquitin chains of RNPS1. We also demonstrate that the catalytic activity of USP4 on ubiquitinated RNPS1 is elevated by squamous cell carcinoma antigen recognized by T cells 3 (Sart3).
authors.affiliation: Department of Biomedical Science, CHA University, Gyeonggi-Do, Korea.
authors.forename: Seul-Ki
authors.initials: SK
authors.lastname: Kwon
authors.affiliation: Department of Biomedical Science, CHA University, Gyeonggi-Do, Korea.
authors.forename: Eun-Hea
authors.initials: EH
authors.lastname: Kim
authors.affiliation: Department of Biomedical Science, CHA University, Gyeonggi-Do, Korea.
authors.forename: Kwang-Hyun
authors.initials: KH
authors.lastname: Baek
mesh_terms: D000951:Antigens, Neoplasm / Q000378:metabolism; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011485:Protein Binding; D055550:Protein Stability; D016601:RNA-Binding Proteins / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism; D043222:Ubiquitin Thiolesterase / Q000378:metabolism*; D064570:Ubiquitin-Specific Proteases; D054875:Ubiquitination
chemical_list: D000951:Antigens, Neoplasm; D016601:RNA-Binding Proteins; C084538:RNPS1 protein, human; D012261:Ribonucleoproteins; C416530:SART3 protein, human; C486203:USP4 protein, human; D025801:Ubiquitin; D043222:Ubiquitin Thiolesterase; D064570:Ubiquitin-Specific Proteases; D046988:Proteasome Endopeptidase Complex
keywords: SR protein; deubiquitinating enzyme; deubiquitination; splicing; ubiquitination