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

doi:10.1242/jcs.00950

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Article

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

Journal of cell science - 1 Mar 2004

Lowe Martin, Lane Jon D, Woodman Philip G, Allan Victoria J

Abstract excerpt

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...

Topics

Animals
Apoptosis
Biological Transport, Active
Caspase 3
Caspases
Endoplasmic Reticulum
Golgi Apparatus
Golgi Matrix Proteins
HeLa Cells
Humans
In Vitro Techniques
Membrane Proteins
Mutagenesis, Site-Directed
Phenotype
Protein Structure, Tertiary
Qa-SNARE Proteins
Rats
Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 14970262
DOI: 10.1242/jcs.00950

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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