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Caspase-7 mediated cleavage of proteasome subunits during apoptosis.

Abstract：

:Caspase-3 and caspase-7 are structurally closely related and demonstrate overlapping substrate specificity. However, during apoptosis, they are differentially regulated and show distinct subcellular localizations, implying the presence of specific substrates. In this study, to identify caspase-7 substrates, we treated the lysates derived from caspase-3-deficient MCF-7 cells with purified caspase-7 and analyzed decreased proteins by 2-DE. Intriguingly, several proteasome subunits such as alpha2, alpha6, and Rpt1 are degraded by caspase-7 during apoptosis in vitro and in vivo. Caspase-7 mediated cleavage of proteasome subunits results in the reduction of proteasome activity and thereby increases the accumulation of ubiquitinated proteins in cells. These findings suggest that caspase-7 facilitates the execution of apoptosis through down-regulation of the 26S proteasome, which regulates the turnover of proteins involved in the apoptotic process.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jang M,Park BC,Lee AY,Na KS,Kang S,Bae KH,Myung PK,Chung BC,Cho S,Lee DH,Park SG

doi

10.1016/j.bbrc.2007.08.183

subject

Has Abstract

pub_date

2007-11-16 00:00:00

pages

388-94

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)01926-2

journal_volume

363

pub_type

杂志文章

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