Deubiquitinating Enzymes as Cellular Regulators

Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26S proteasome. Deubiquitination, reversal of this modification, must also regulate the fate and function of ubiquitin-conjugated proteins. D...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 2003-07, Vol.134 (1), p.9-18
Main Authors: Kim, Jung Hwa, Park, Kyung Chan, Chung, Sung Soo, Bang, Oksun, Chung, Chin Ha
Format: Article
Language:English
Subjects:
Animals
Cysteine Endopeptidases - chemistry
Cysteine Endopeptidases - physiology
Endopeptidases - chemistry
Endopeptidases - physiology
Humans
JAMM
Key words: deubiquitinating enzyme
Multienzyme Complexes - chemistry
Multienzyme Complexes - physiology
otubain
Transcription, Genetic
ubiquitin C-terminal hydrolase
Ubiquitin Thiolesterase - chemistry
Ubiquitin Thiolesterase - physiology
ubiquitin-specific processing protease
Ubiquitins - metabolism
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26S proteasome. Deubiquitination, reversal of this modification, must also regulate the fate and function of ubiquitin-conjugated proteins. Deubiquitinating enzymes catalyze the removal of ubiquitin from ubiquitin-conjugated substrate proteins as well as from its precursor proteins. Deubiquitinating enzymes occupy the largest family of enzymes in the ubiquitin system, implying their diverse function in regulation of the ubiquitin-mediated pathways. Here we explore the diversity of deubiquitinating enzymes and their emerging roles as cellular regulators.
ISSN:0021-924X
DOI:10.1093/jb/mvg107