期刊
BIOCHEMICAL JOURNAL
卷 414, 期 -, 页码 161-175出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20080798
关键词
deubiquitinating enzyme (DUB); deubiquitination; proteasome; ubiquitin; ubiquitin-specific protease
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM030308] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM030308-27, R01 GM030308] Funding Source: Medline
Protein modification by ubiquitin and ubiquitin-like molecules is a critical regulatory process. Like most regulated protein modifications, ubiquitination is reversible. Deubiquitination, the reversal of ubiquitination, is quickly being recognized as an important regulatory strategy. Nearly one hundred human DUBS (deubiquitinating enzymes) in five different gene families oppose the action of several hundred ubiquitin ligases, suggesting that both ubiquitination and its reversal are highly regulated and specific processes. It has long been recognized that ubiquitin ligases are modular enzyme systems that often depend on scaffolds and adaptors to deliver Substrates to the catalytically active macromolecular complex. Although many DUBS bind ubiquitin with reasonable affinities (in the nM to mu M range), a larger number have little affinity but exhibit robust catalytic capability. Thus it is apparent that these DUBS Must acquire their Substrates by binding the target protein in a conjugate or by associating with other macromolecular complexes. We Would then expect that a study of protein partners of DUBS would reveal a variety Of Substrates, scaffolds, adaptors and ubiquitin receptors. In the present review We Suggest that, like ligases, much of the regulation and specificity of deubiquitination arises from the association of DUBs with these protein partners.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据