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CHFR binds to and regulates MAD2 in the spindle checkpoint through its cysteine-rich domain.

Abstract：

:CHFR has been implicated as a tumor suppressor in a multitude of cancers. It was originally identified as a major component of the antephase checkpoint. Recently, CHFR was reported to interact with MAD2, an important component of the spindle assembly checkpoint, where CHFR knockdown resulted in mislocalization of MAD2 and disruption of the MAD2/CDC20 interaction. To further understand how CHFR interacts with MAD2, we deleted key functional domains of CHFR, and investigated the effect on MAD2 binding and function. Here we show that deletion of the cysteine-rich domain of CHFR is required for the CHFR/MAD2 interaction as well as proper localization of MAD2 in the cell. Furthermore, the cysteine-rich domain deletion exhibits impaired ability to promote the MAD2/CDC20 interaction, leading to an increase in mitotic defects relative to wild type CHFR. These data support a critical role for CHFR in the MAD2 spindle checkpoint. Furthermore, these data establish the cysteine-rich domain of CHFR as the essential domain for the CHFR/MAD2 interaction and for promoting interaction between MAD2 and CDC20 to inhibit the anaphase-promoting complex.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Keller JA,Petty EM

doi

10.1016/j.bbrc.2011.04.143

subject

Has Abstract

pub_date

2011-06-10 00:00:00

pages

389-93

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)00752-2

journal_volume

409

pub_type

杂志文章

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