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Deubiquitinating enzymes: their diversity and emerging roles.

Abstract：

:A growing number of important regulatory proteins within cells are modified by conjugation of ubiquitin, a well-conserved 76-amino-acid polypeptide. The ubiquitinated proteins are targeted to proteasome for degradation or alternative metabolic fates, such as triggering of plasma membrane endocytosis and trafficking to vacuoles or lysosomes. Deubiquitination, reversal of this modification, is being recognized as an important regulatory step. Deubiquitinating enzymes are cysteine proteases that specifically cleave off ubiquitin from ubiquitin-conjugated protein substrates as well as from its precursor proteins. Genome sequencing projects have identified more than 90 deubiquitinating enzymes, making them the largest family of enzymes in the ubiquitin system. This review will concentrate on recent important findings as well as new insights into the diversity and emerging roles of deubiquitinating enzymes in the ubiquitin-dependent pathway.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Chung CH,Baek SH

doi

10.1006/bbrc.1999.1880

subject

Has Abstract

pub_date

1999-12-29 00:00:00

pages

633-40

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)91880-6

journal_volume

266

pub_type

杂志文章,评审

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