The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Deubiquitinating Enzymes as Cellular Regulators
Jung Hwa KimKyung Chan ParkSung Soo ChungOksun BangChin Ha Chung
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2003 Volume 134 Issue 1 Pages 9-18

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Abstract

Modification of proteins by the covalent attachment of ubiquitin is a key regulatory mechanism of many cellular processes including protein degradation by the 26 S 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.

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© The Japanese Biochemical Society
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