Golgi fragmentation during Fas-mediated apoptosis is associated with the rapid loss of GM130.
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.
Centre for Inflammation Research, The University of Edinburgh, Medical School, Teviot Place, Edinburgh EH8 9AG, UK. awalker4@staffmail.ed.ac.uk
Annemieke
A
Walker
Carol
C
Ward
Tara A
TA
Sheldrake
Ian
I
Dransfield
Adriano G
AG
Rossi
James G
JG
Pryde
Christopher
C
Haslett
D017209:Apoptosis; D001324:Autoantigens; D002460:Cell Line; D004791:Enzyme Inhibitors / Q000633:toxicity; D005455:Fluorescent Antibody Technique; D006056:Golgi Apparatus / Q000648:ultrastructure*; D006801:Humans; D019169:Jurkat Cells; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D047428:Protein Kinase Inhibitors; D019311:Staurosporine / Q000633:toxicity; D019014:fas Receptor / Q000378:metabolism*
D001324:Autoantigens; D004791:Enzyme Inhibitors; C097741:Golgin subfamily A member 2; D008565:Membrane Proteins; D047428:Protein Kinase Inhibitors; D019014:fas Receptor; D019311:Staurosporine