NDLI: Preferential digestion of PCNA-ubiquitin and p53-ubiquitin linkages by USP7 to remove polyubiquitin chains from substrates

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Preferential digestion of PCNA-ubiquitin and p53-ubiquitin linkages by USP7 to remove polyubiquitin chains from substrates

Content Provider	Journal of Biological Chemistry (JBC)
Author	Masuda, Yuji Kanao, Rie Kawai, Hidehiko Kukimoto, Iwao Masutani, Chikahide
Abstract	Ubiquitin-specific protease 7 (USP7) regulates various cellular pathways through its deubiquitination activity. Despite the identification of a growing number of substrates of USP7, the molecular mechanism by which USP7 removes ubiquitin chains from polyubiquitinated substrates remains unexplored. The present study investigated the mechanism underlying the deubiquitination of K63-linked polyubiquitinated proliferating cell nuclear antigen (PCNA). Biochemical analyses demonstrated that USP7 efficiently removes polyubiquitin chains from polyubiquitinated PCNA by preferential cleavage of the PCNA-ubiquitin linkage. This property was largely attributed to the poor activity towards K63-linked ubiquitin chains. The preferential cleavage of substrate-ubiquitin linkages was also observed for K48-linked polyubiquitinated p53 because of the inefficient cleavage of the K48-linked ubiquitin chains. The present findings suggest a mechanism underlying the removal of polyubiquitin signals by USP7.
Related Links	http://www.jbc.org/content/early/2019/01/15/jbc.RA118.005167.abstract
Starting Page	jbc.RA118.005167
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
DOI	10.1074/jbc.RA118.005167
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2019-01-15
Access Restriction	Open
Subject Keyword	Enzyme kinetics Proliferating cell nuclear antigen (PCNA) DNA damage response P53 Deubiquitylation (deubiquitination) Enzymology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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