Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.
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.
Kayalar
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La Jolla Cancer Research Foundation, CA 92037, USA.
Ord
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Testa
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Zhong
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Bredesen
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D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D017209:Apoptosis; D020170:Caspase 1; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism; D016716:PC12 Cells; D010449:Peptide Mapping; D011485:Protein Binding; D051381:Rats; D013379:Substrate Specificity
D000199:Actins; D007375:Interleukin-1; D003546:Cysteine Endopeptidases; D020170:Caspase 1