Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin

	Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin
	Zhang, YH; Zhou, CJ; Zhou, ZR; Song, AX; Hu, HY
刊名	PLOS ONE
	2011
卷号	6 期号:12 页码:e29362-e29362
通讯作者	Zhang, YH (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai, Peoples R China.,hyhu@sibs.ac.cn
英文摘要	Deubiquitination is a reverse process of cellular ubiquitination important for many biological events. Ubiquitin (Ub)-specific protease 13 (USP13) is an ortholog of USP5 implicated in catalyzing hydrolysis of various Ub chains, but its enzymatic properties and catalytic regulation remain to be explored. Here we report studies of the roles of the Ub-binding domains of USP13 in regulatory catalysis by biochemical and NMR structural approaches. Our data demonstrate that USP13, distinct from USP5, exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin (K63-polyUb) in a non-activation manner. The zinc finger (ZnF) domain of USP13 shares a similar fold with that of USP5, but it cannot bind with Ub, so that USP13 has lost its ability to be activated by free Ub. Substitution of the ZnF domain with that of USP5 confers USP13 the property of catalytic activation. The tandem Ub-associated (UBA) domains of USP13 can bind with different types of diUb but preferentially with K63-linked, providing a possible explanation for the weak activity preferring to K63-polyUb. USP13 can also regulate the protein level of CD3 delta in cells, probably depending on its weak deubiquitinating activity and the Ub-binding properties of the UBA domains. Thus, the non-activating catalysis of USP13 for K63-polyUb chains implies that it may function differently from USP5 in cellular deubiquitination processes.
学科主题	Science & Technology - Other Topics
类目[WOS]	Multidisciplinary Sciences
关键词[WOS]	UBIQUITIN-BINDING DOMAINS ; ISOPEPTIDASE-T ; PROTEIN-DEGRADATION ; ENDOPLASMIC-RETICULUM ; CHAINS ; PROTEASOME ; ZINC ; UBP ; RECOGNITION ; MECHANISM
收录类别	SCI
语种	英语
WOS记录号	WOS:000300676300050
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/870]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Zhang, YH,Zhou, CJ,Zhou, ZR,et al. Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin[J]. PLOS ONE,2011,6(12):e29362-e29362.
APA	Zhang, YH,Zhou, CJ,Zhou, ZR,Song, AX,&Hu, HY.(2011).Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin.PLOS ONE,6(12),e29362-e29362.
MLA	Zhang, YH,et al."Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin".PLOS ONE 6.12(2011):e29362-e29362.