Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The mammalian Golgi complex is comprised of a ribbon of stacked cisternal membranes often located in the pericentriolar region of the cell. Here, we report that during apoptosis the Golgi ribbon is fragmented into dispersed clusters of tubulo-vesicular membranes. We have found that fragmentation is caspase dependent and identified GRASP65 (Golgi reassembly and stacking protein of 65 kD) as a novel caspase substrate. GRASP65 is cleaved specifically by caspase-3 at conserved sites in its membrane distal COOH terminus at an early stage of the execution phase. Expression of a caspase-resistant form of GRASP65 partially preserved cisternal stacking and inhibited breakdown of the Golgi ribbon in apoptotic cells. Our results suggest that GRASP65 is an important structural component required for maintenance of Golgi apparatus integrity.

Original publication

DOI

10.1083/jcb.200110007

Type

Journal article

Journal

J Cell Biol

Publication Date

04/02/2002

Volume

156

Pages

495 - 509

Keywords

Amino Acid Chloromethyl Ketones, Apoptosis, Autoantigens, Caspase 3, Caspases, Enzyme Inhibitors, Glycoproteins, Golgi Apparatus, Green Fluorescent Proteins, HeLa Cells, Humans, Luminescent Proteins, Membrane Glycoproteins, Membrane Proteins, Microscopy, Electron, Microscopy, Fluorescence, Microscopy, Video, N-Acetylgalactosaminyltransferases, Oligopeptides, Peptide Hydrolases, Proteins