Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis

Cell. 1998 Sep 18;94(6):783-93. doi: 10.1016/s0092-8674(00)81737-7.

Abstract

Mitotic fragmentation of the Golgi apparatus can be largely explained by disruption of the interaction between GM130 and the vesicle-docking protein p115. Here we identify a single serine (Ser-25) in GM130 as the key phosphorylated target and Cdc2 as the responsible kinase. MEK1, a component of the MAP kinase signaling pathway recently implicated in mitotic Golgi fragmentation, was not required for GM130 phosphorylation or mitotic fragmentation either in vitro or in vivo. We propose that Cdc2 is directly involved in mitotic Golgi fragmentation and that signaling via MEK1 is not required for this process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autoantigens
  • CDC2 Protein Kinase / metabolism*
  • Golgi Apparatus / chemistry
  • Golgi Apparatus / enzymology*
  • Guanine Nucleotide Exchange Factors
  • HeLa Cells
  • Humans
  • MAP Kinase Kinase 1
  • Membrane Proteins / metabolism*
  • Mitogen-Activated Protein Kinase Kinases*
  • Mitosis / physiology*
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding / physiology
  • Protein-Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Serine / metabolism

Substances

  • Autoantigens
  • Golgin subfamily A member 2
  • Guanine Nucleotide Exchange Factors
  • Membrane Proteins
  • Proteins
  • Serine
  • Protein-Tyrosine Kinases
  • Protein-Serine-Threonine Kinases
  • CDC2 Protein Kinase
  • MAP Kinase Kinase 1
  • MAP2K1 protein, human
  • Mitogen-Activated Protein Kinase Kinases

Associated data

  • GENBANK/U35022