GRASP65, a Protein Involved in the Stacking of Golgi Cisternae


NEM prevents mitotic reassembly of Golgi cisternae into stacked structures. The major target of NEM is a 65 kDa protein conserved from yeast to mammals. Antibodies to this protein and a recombinant form of it block cisternal stacking in a cell-free system, justifying its designation as a Golgi ReAssembly Stacking Protein (GRASP65). One of the two minor targets of NEM is GM130, previously implicated in the docking of transport vesicles and mitotic fragmentation of the Golgi stack. GRASP65 is complexed with GM130 and is tightly bound to Golgi membranes, even under mitotic conditions when both are heavily phosphorylated. These results link vesicle docking, stacking of Golgi cisternae, and the disruption of both of these interactions during mitosis.

DOI: 10.1016/S0092-8674(00)80407-9

Extracted Key Phrases

4 Figures and Tables

Citations per Year

1,413 Citations

Semantic Scholar estimates that this publication has 1,413 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Barr1997GRASP65AP, title={GRASP65, a Protein Involved in the Stacking of Golgi Cisternae}, author={Francis A Barr and Magda Puype and Jo{\"{e}l Vandekerckhove and Graham S. Warren}, journal={Cell}, year={1997}, volume={91}, pages={253-262} }