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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Caspase- mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis.

We report the caspase-dependent cleavage of two Golgi-associated transport factors during apoptosis. The tethering factor giantin is rapidly cleaved both in vitro and in vivo at a conserved site, to generate a stable membrane-anchored domain and a soluble domain that is subject to further caspase-dependent cleavage. The t-SNARE syntaxin 5 is also cleaved rapidly, resulting in the separation of the catalytic membrane-proximal domain from an N-terminal regulatory domain. Cleavage of giantin and syntaxin 5 is accompanied by a cessation of vesicular transport between the ER and the Golgi complex, which first manifests itself as a block in ER exit. The contribution that such an inhibition of trafficking may make towards the generation of an apoptotic phenotype is discussed.[1]

References

  1. Caspase-mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis. Lowe, M., Lane, J.D., Woodman, P.G., Allan, V.J. J. Cell. Sci. (2004) [Pubmed]
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