PIAS3 induces SUMO‐1 modification and transcriptional repression of IRF‐1

FEBS Letters

Nakagawa, Koji¹  Yokosawa, Hideyoshi¹ 

[1] Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan

关键词: Interferon regulatory factor-1;    Protein inhibitor of activated STAT3;    Small ubiquitin-related modifier-1 ligase;    Small ubiquitin-related modifier-1 modification;    Transcriptional repression;    IRF-1;    interferon regulatory factor-1;    PIAS3;    protein inhibitor of activated STAT3;    SUMO-1;    small ubiquitin-related modifier-1;    Ubc9;    ubiquitin-conjugating enzyme 9;    PCR;    polymerase chain reaction;    ISRE;    interferon-stimulated response element;   

DOI  :  10.1016/S0014-5793(02)03486-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interferon regulatory factor-1 (IRF-1) is a transcriptional activator that is involved in interferon response, regulation of cell growth and oncogenesis. To try to identify the molecules that regulate the function of IRF-1, we performed yeast two-hybrid screening and isolated protein inhibitor of activated STAT3 (PIAS3) as an IRF-1-binding protein. This protein was also found to bind with small ubiquitin-related modifier-1 (SUMO-1) and ubiquitin-conjugating enzyme 9, an E2 in the SUMO-1-conjugating system. Co-expression of PIAS3 induced SUMO-1 modification of IRF-1 in a RING finger domain-dependent manner and also repressed transcriptional activity of IRF-1. Thus, PIAS3 functions as a SUMO-1 ligase for IRF-1 and also as a repressor of IRF-1 transcriptional activity.

【 授权许可】

Unknown