USE1 is a bispecifi c conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis

被引：83

作者：

Aichem, Annette ^{[1
]}

Pelzer, Christiane ^{[2
]}

Lukasiak, Sebastian ^{[2
]}

Kalveram, Birte ^{[2
]}

Sheppard, Paul W. ^{[3
]}

Rani, Neha ^{[2
]}

Schmidtke, Gunter ^{[2
]}

Groettrup, Marcus ^{[1
,2
]}

机构：

[1] Univ Konstanz, Biotechnol Inst Thurgau, CH-8280 Kreuzlingen, Switzerland

[2] Univ Konstanz, Div Immunol, Dept Biol, D-78457 Constance, Germany

[3] Enzo Life Sci UK Ltd, Exeter EX2 8NL, Devon, England

来源：

NATURE COMMUNICATIONS | 2010年 / 1卷

关键词：

PROTEIN FAT10; CRYSTAL-STRUCTURE; MODIFIER FAT10; E2; ENZYME; DEGRADATION; BINDING; SYSTEM; ISG15; E1; IDENTIFICATION;

D O I：

10.1038/ncomms1012

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The ubiquitin-like modifi er FAT10 targets proteins for degradation by the proteasome and is activated by the E1 enzyme UBA6. In this study, we identify the UBA6-specific E2 enzyme (USE1) as an interaction partner of FAT10. Activated FAT10 can be transferred from UBA6 onto USE1 in vitro, and endogenous USE1 and FAT10 can be coimmunoprecipitated from intact cells. Small interfering RNA-mediated downregulation of USE1 mRNA resulted in a strong reduction of FAT10 conjugate formation under endogenous conditions, suggesting that USE1 is a major E2 enzyme in the FAT10 conjugation cascade. Interestingly, USE1 is not only the first E2 enzyme but also the first known substrate of FAT10 conjugation, as it was efficiently auto-FAT10ylated in cis but not in trans

引用

页数：10

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