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CACUL1/CAC1 attenuates p53 activity through PML post-translational modification.

Abstract：

:Promyelocytic leukaemia (PML) is a tumor suppressor protein covalently conjugated with SUMO family proteins, leading to the formation of PML nuclear bodies (NBs). PML-NBs provide a platform for efficient posttranslational modification of targets and protein-protein interaction, contributing to the adjustment of gene expression and chromatin integrity. Although PML SUMOylation is thought to play important roles in diverse cellular functions, the control mechanisms of adequate modification levels have remained unsolved. Here, we report that Cullin-related protein CACUL1/CAC1 (CACUL1) inhibits PML posttranslational modification. CACUL1 interacts with PML and suppresses PML SUMOylation, leading to the regulation of PML-NB size in the nucleus. We also found that Ubc9, a SUMO-conjugating enzyme, binds to CACUL1 and antagonizes the interaction between CACUL1 and PML. Furthermore, CACUL1 attenuates p53 transcriptional activity. These data suggest that CACUL1 is a novel regulator that negatively controls p53 activity through the regulation of PML SUMOylation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Fukuda T,Kigoshi-Tansho Y,Naganuma T,Kazaana A,Okajima T,Tsuruta F,Chiba T

doi

10.1016/j.bbrc.2016.11.125

subject

Has Abstract

pub_date

2017-01-22 00:00:00

pages

863-869

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)31999-4

journal_volume

482

pub_type

杂志文章

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