Involvement of PIAS1 in the sumoylation of tumor suppressor p53

被引：447

作者：

Kahyo, T ^{[1
]}

Nishida, T ^{[1
]}

Yasuda, H ^{[1
]}

机构：

[1] Tokyo Univ Pharm & Life Sci, Sch Life Sci, Tokyo 1920392, Japan

来源：

MOLECULAR CELL | 2001年 / 8卷 / 03期

关键词：

D O I：

10.1016/S1097-2765(01)00349-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Sumoylation of p53 by the ubiquitin-like protein, SUMO-1/ sentrin/PIC1, has been shown to stimulate its transcriptional activation activity. The SUMO E3 ligase, a key enzyme in the recognition of substrates to be sumoylated, has not yet been identified. We isolated PIAS1 (protein inhibitor of activated STAT1) as a SUMO-1 binding protein by yeast two-hybrid screening. In addition, PIAS1 bound p53 and Ubc9, the E2 for SUMO. PIAS1 that was mutated in the RING finger-like domain bound p53 and SUMO-1, but not Ubc9. PIAS1 catalyzed the sumoylation of p53 both in U2OS cells and in vitro in a domain-dependent manner. These data suggest that PIAS1 functions as a SUMO ligase, or possibly as a tightly bound regulator of it, toward p53.

引用

页码：713 / 718

页数：6

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