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Cell cycle regulation of the BRCA1/acetyl-CoA-carboxylase complex.

Abstract：

:Germ-line alterations in BRCA1 are associated with an increased susceptibility to breast and ovarian cancer. The BRCA1 protein has been implicated in multiple cellular functions. We have recently demonstrated that BRCA1 reduces acetyl-CoA-carboxylase alpha (ACCA) activity through its phospho-dependent binding to ACCA, and further established that the phosphorylation of the Ser1263 of ACCA is required for this interaction. Here, to gain more insight into the cellular conditions that trigger the BRCA1/ACCA interaction, we designed an anti-pSer1263 antibody and demonstrated that the Ser1263 of ACCA is phosphorylated in vivo, in a cell cycle-dependent manner. We further showed that the interaction between BRCA1 and ACCA is regulated during cell cycle progression. Taken together, our findings reveal a novel mechanism of regulation of ACCA distinct from the previously described phosphorylation of Ser79, and provide new insights into the control of lipogenesis through the cell cycle.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ray H,Suau F,Vincent A,Dalla Venezia N

doi

10.1016/j.bbrc.2008.11.090

subject

Has Abstract

pub_date

2009-01-16 00:00:00

pages

615-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02298-5

journal_volume

378

pub_type

杂志文章

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