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. 1996 Mar 5;93(5):2234-8.
doi: 10.1073/pnas.93.5.2234.

Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition

C Kayalar  1 , T Ord, M P Testa, L T Zhong, D E Bredesen
Affiliations

Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition

C Kayalar et al. Proc Natl Acad Sci U S A. .

Abstract

Three of the predominant features of apoptosis are internucleosomal DNA fragmentation, plasma membrane bleb formation, and retraction of cell processes. We demonstrate that actin is a substrate for the proapoptotic cysteine protease interleukin 1beta-converting enzyme. Actin cleaved by interleukin 1beta-converting enzyme can neither inhibit DNase I nor polymerize to its filamentous form as effectively as intact actin. These findings suggest a mechanism for the coordination of the proteolytic, endonucleolytic, and morphogenetic aspects of apoptosis.

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