PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73.

ABSTRACT: p73 is a recently described member of the p53 family, and, like p53, it undergoes a number of posttranslational modifications. Here we show, by yeast two-hybrid screening, pull-down assays, and coimmunoprecipitation, that p73alpha, -beta, and -gamma bind to the protein inhibitor of activated STAT-1 (PIAS-1) and that this binding stabilizes p73. PIAS-1 also sumoylates p73alpha, although not the C-terminally truncated isoforms p73beta and -gamma, and this requires the RING finger domain of PIAS-1. The DeltaNp73alpha isoform can also bind, and be sumoylated by, PIAS-1. PIAS-1-mediated sumoylation decreases p73 transcriptional activity on several target promoters, such as Bax. p73 is colocalized in the nucleus with PIAS-1, and sumoylated p73 is located exclusively in the nuclear matrix. PIAS-1

SUBMITTER: Munarriz E 

PROVIDER: S-EPMC533962 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature