Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells

Cell. 2002 May 3;109(3):359-69. doi: 10.1016/s0092-8674(02)00720-1.


The pericentriolar Golgi stacks are fragmented and found dispersed in mitotic mammalian cells. Addition of an antibody to the Golgi-associated protein GRASP65 inhibited Golgi fragmentation by mitotic cytosol in permeabilized cells. Microinjecting this antibody or the C-terminal fragment of GRASP65, which contains the antibody binding site, into normal rat kidney cells prevented entry into mitosis. Under these conditions the cells had completed S phase but were not in the prophase stage of mitosis. Fragmentation of the Golgi apparatus by nocodazole or Brefeldin A treatment prior to or post microinjection of the anti-GRASP65 antibody alleviated the block in mitotic entry. Based on our findings, we suggest that the pericentriolar Golgi organization is a sensor for controlling entry into mitosis in mammalian cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aphidicolin / pharmacology
  • Binding Sites
  • Biomarkers
  • Brefeldin A / pharmacology
  • Cells, Cultured
  • Centrioles / metabolism
  • Centrioles / physiology*
  • Epitopes / metabolism
  • Golgi Apparatus / drug effects
  • Golgi Apparatus / metabolism
  • Golgi Apparatus / physiology*
  • Golgi Matrix Proteins
  • Kidney / cytology
  • Kidney / metabolism*
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / metabolism
  • Mitosis / drug effects
  • Mitosis / physiology*
  • Nocodazole / pharmacology
  • Protein Structure, Tertiary
  • Rats
  • Recombinant Proteins / metabolism


  • Biomarkers
  • Epitopes
  • Golgi Matrix Proteins
  • Gorasp1 protein, rat
  • Membrane Proteins
  • Recombinant Proteins
  • Brefeldin A
  • Aphidicolin
  • Nocodazole