GRASP65, a protein involved in the stacking of Golgi cisternae

Cell. 1997 Oct 17;91(2):253-62. doi: 10.1016/s0092-8674(00)80407-9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Autoantigens
  • Base Sequence
  • Cell Cycle / physiology
  • Cell-Free System
  • Conserved Sequence*
  • Ethylmaleimide / pharmacology
  • Golgi Apparatus / chemistry*
  • Golgi Apparatus / drug effects
  • Golgi Apparatus / metabolism
  • Golgi Matrix Proteins
  • HeLa Cells
  • Humans
  • Male
  • Membrane Proteins / analysis
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism*
  • Mitosis / physiology
  • Molecular Sequence Data
  • Myristates / metabolism
  • Phosphorylation
  • Rats
  • Rats, Sprague-Dawley
  • Sequence Homology, Amino Acid


  • Autoantigens
  • GORASP1 protein, human
  • Golgi Matrix Proteins
  • Golgin subfamily A member 2
  • Gorasp1 protein, rat
  • Membrane Proteins
  • Myristates
  • Ethylmaleimide

Associated data

  • GENBANK/AF015264