Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis.

Abstract:

:Cytochrome C is a mitochondrial protein that induces apoptosis when released into the cytosol or when added to cell-free extracts. Here we show that cells that overexpress the Bcl-2-related protein Bcl-xL fail to accumulate cytosolic cytochrome C or undergo apoptosis in response to genotoxic stress. Coimmunoprecipitation studies demonstrate that Bcl-xL associates with cytochrome C. Cytochrome C binds directly and specifically to Bcl-xL and not to the proapoptotic Bcl-xs protein. The results also demonstrate that Bcl-xs blocks binding of cytochrome C to Bcl-xL. Our findings support a role for Bcl-xL in protecting cells from apoptosis by inhibiting the availability of cytochrome C in the cytosol.

authors

Kharbanda S,Pandey P,Schofield L,Israels S,Roncinske R,Yoshida K,Bharti A,Yuan ZM,Saxena S,Weichselbaum R,Nalin C,Kufe D

doi

10.1073/pnas.94.13.6939

subject

Has Abstract

pub_date

1997-06-24 00:00:00

pages

6939-42

issue

13

eissn

0027-8424

issn

1091-6490

journal_volume

94

pub_type

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