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Biochem Biophys Res Commun. 2004 Mar 26;316(1):6-11.

Golgi fragmentation during Fas-mediated apoptosis is associated with the rapid loss of GM130.

Author information

1
Centre for Inflammation Research, The University of Edinburgh, Medical School, Teviot Place, Edinburgh EH8 9AG, UK. awalker4@staffmail.ed.ac.uk

Abstract

During apoptosis, the Golgi complex becomes fragmented and key proteins (e.g., GRASP65 and p115) are targets for caspase cleavage. GM130, an integral membrane protein, contributes to the maintenance of Golgi structure and facilitates membrane fusion with secretory vesicles. We show that GM130 levels decrease during Fas-induced apoptosis but not during staurosporine-induced apoptosis while in both models p115 levels remain unaffected. We conclude that GM130 is rapidly diminished during Fas-mediated apoptosis associated with Golgi fragmentation in contrast to previous studies which have suggested that loss of GM130 during apoptosis is a late event.

PMID:
15003503
DOI:
10.1016/j.bbrc.2004.02.015
[Indexed for MEDLINE]

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