Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.
C Kayalar, T Ord, MP Testa… - Proceedings of the …, 1996 - National Acad Sciences
C Kayalar, T Ord, MP Testa, LT Zhong, DE Bredesen
Proceedings of the National Academy of Sciences, 1996•National Acad SciencesThree 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 …
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 …
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.
National Acad Sciences