Abstract
Caspases are the proteases that transduce proapoptotic signals in cells. Mancini et al. show that caspase-2 localizes primarily to the cytoplasmic face of the Golgi complex. Casapse-2 cleaved golgin-160, a Golgi membrane protein implicated in maintaining Golgi integrity and membrane trafficking. When a noncleavable mutant form of golgin-160 was overexpressed in cultured cells, Golgi disintegration was delayed in response to apoptosis-inducing agents. The data support the notion that particular caspases may localize to specific intracellular sites to interact with specific substrates and to generate distinct apoptotic signals. Mancini, M., Machamer, C.E., Roy, S., Nicholson, D.W., Thornberry, N.A., Casciola-Rosen, L.A., and Rosen, A. (2000) Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J. Cell Biol. 149 : 603-612. [Abstract] [Full Text]
Published Version
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