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• W2564590854 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)." @default.
• W2564590854 created "2017-01-06" @default.
• W2564590854 creator A5035940528 @default.
• W2564590854 creator A5036560565 @default.
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• W2564590854 date "2017-01-01" @default.
• W2564590854 modified "2023-09-27" @default.
• W2564590854 title "RNPS1 is modulated by ubiquitin-specific protease 4" @default.
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• W2564590854 doi "https://doi.org/10.1002/1873-3468.12531" @default.
• W2564590854 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27990632" @default.
• W2564590854 hasPublicationYear "2017" @default.
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