Premium
The co‐chaperone p23 is degraded by caspases and the proteasome during apoptosis
Author(s) -
Mollerup Jens,
Berchtold Martin W.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.045
Subject(s) - apoptosis , staurosporine , proteasome , caspase , microbiology and biotechnology , chaperone (clinical) , chemistry , hsp70 , intrinsic apoptosis , heat shock protein , biochemistry , biology , programmed cell death , phosphorylation , protein kinase c , medicine , gene , pathology
The heat shock protein 90 co‐chaperone p23 has recently been shown to be up‐regulated in cancer cells and down‐regulated in atheroschlerotic plaques. We found that p23 is degraded during apoptosis induced by several stimuli, including Fas and TNFα‐receptor activation as well as staurosporine treatment. Caspase inhibition protected p23 from degradation in several cell lines. In addition, recombinant caspase‐3 and 8 cleaved p23 at Asp 142 generating a degradation product of 18 kDa as seen in apoptotic cells. Truncated p23 is further degraded in a proteasome dependent process during apoptosis. Furthermore, we found that the anti‐aggregating activity of truncated p23 was reduced compared to full length p23 indicating that caspase mediated p23 degradation contributes to protein destabilisation in apoptosis.