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. 1996 Mar 5;93(5):2234–2238. 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 1, M P Testa 1, L T Zhong 1, D E Bredesen 1
PMCID: PMC39941  PMID: 8700913

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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