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. 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.
Kim
Jung Hwa
JH
NRL of Protein Biochemistry, School of Biological Sciences, Seoul National University, Seoul 151-742, Korea.
Park
Kyung Chan
KC
Chung
Sung Soo
SS
Bang
Oksun
O
Chung
Chin Ha
CH
D000818:Animals; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000502:physiology*; D010450:Endopeptidases / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D009097:Multienzyme Complexes / Q000737:chemistry / Q000502:physiology*; D014158:Transcription, Genetic; D043222:Ubiquitin Thiolesterase / Q000737:chemistry / Q000502:physiology*; D014452:Ubiquitins / Q000378:metabolism*
D009097:Multienzyme Complexes; D014452:Ubiquitins; D010450:Endopeptidases; D043222:Ubiquitin Thiolesterase; D003546:Cysteine Endopeptidases; C059237:ubiquitin-Nalpha-protein hydrolase