Journal
JOURNAL OF CELL BIOLOGY
Volume 149, Issue 3, Pages 603-612Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.149.3.603
Keywords
signaling; subcellular; substrate; coiled coil; protease
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Funding
- NIAMS NIH HHS [R01 AR044684, AR44684] Funding Source: Medline
- NIDCR NIH HHS [R37 DE012354, DE12354, R01 DE012354] Funding Source: Medline
- NIGMS NIH HHS [GM42522, R01 GM042522] Funding Source: Medline
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Caspases are an extended family of cysteine proteases that play critical roles in apoptosis. Animals deficient in caspases-2 or -3, which share very similar tetrapeptide cleavage specificities, exhibit very different phenotypes, suggesting that the unique features of individual caspases may account for distinct regulation and specialized functions. Recent studies demonstrate that unique apoptotic stimuli are transduced by distinct proteolytic pathways, with multiple components of the proteolytic machinery clustering at distinct subcellular sites. We demonstrate here that, in addition to its nuclear distribution, caspase-2 is localized to the Golgi complex, where it cleaves golgin-160 at a unique site not susceptible to cleavage by other caspases with very similar tetrapeptide specificities. Early cleavage at this site precedes cleavage at distal sites by other caspases. Prevention of cleavage at the unique caspase-2 site delays disintegration of the Golgi complex after delivery of a pro-apoptotic signal. We propose that the Golgi complex, like mitochondria, senses and integrates unique local conditions, and transduces pro-apoptotic signals through local caspases, which regulate local effectors.
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