The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner

Cell. 1997 May 2;89(3):445-55. doi: 10.1016/s0092-8674(00)80225-1.


The docking of transport vesicles with their target membrane is thought to be mediated by p115. We show here that GM130, a cis-Golgi matrix protein, interacts specifically with p115 and so could provide a membrane docking site. Deletion analysis showed that the N-terminus binds to p115, whereas the C-terminus binds to Golgi membranes. Mitotic phosphorylation of GM130 or a peptide derived from the N-terminus prevented binding to p115. The peptide also inhibited the NSF- but not the p97-dependent reassembly of Golgi cisternae from mitotic fragments, unless it was mitotically phosphorylated. Together, these data provide a molecular explanation for the COPI-mediated fragmentation of the Golgi apparatus at the onset of mitosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Autoantigens
  • Carrier Proteins / metabolism*
  • Cell Line / physiology
  • Golgi Apparatus / chemistry
  • Golgi Apparatus / metabolism*
  • Golgi Matrix Proteins
  • Kidney / cytology
  • Liver / chemistry
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mitosis / physiology*
  • Molecular Sequence Data
  • Octoxynol
  • Peptide Fragments / metabolism
  • Protein Binding / physiology
  • Protein Structure, Tertiary
  • Rats
  • Salts
  • Vesicular Transport Proteins*


  • Autoantigens
  • Carrier Proteins
  • Golgi Matrix Proteins
  • Golgin subfamily A member 2
  • Membrane Proteins
  • Peptide Fragments
  • Salts
  • Vesicular Transport Proteins
  • vesicular transport factor p115
  • Octoxynol

Associated data

  • GENBANK/U35022