GRASP65, a protein involved in the stacking of Golgi cisternae

  • Barr F
  • Puype M
  • Vandekerckhove J
 et al. 
  • 91

    Readers

    Mendeley users who have this article in their library.
  • 282

    Citations

    Citations of this article.

Abstract

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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Francis A. Barr

  • Magda Puype

  • Joël Vandekerckhove

  • Graham Warren

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free