GMAP-210, A cis-Golgi network-associated protein, is a minus end microtubule-binding protein

J Cell Biol. 1999 Apr 5;145(1):83-98. doi: 10.1083/jcb.145.1.83.


We report that a peripheral Golgi protein with a molecular mass of 210 kD localized at the cis-Golgi network (Rios, R.M., A.M. Tassin, C. Celati, C. Antony, M.C. Boissier, J.C. Homberg, and M. Bornens. 1994. J. Cell Biol. 125:997-1013) is a microtubule-binding protein that associates in situ with a subpopulation of stable microtubules. Interaction of this protein, now called GMAP-210, for Golgi microtubule-associated protein 210, with microtubules in vitro is direct, tight and nucleotide-independent. Biochemical analysis further suggests that GMAP-210 specifically binds to microtubule ends. The full-length cDNA encoding GMAP-210 predicts a protein of 1, 979 amino acids with a very long central coiled-coil domain. Deletion analyses in vitro show that the COOH terminus of GMAP-210 binds to microtubules whereas the NH2 terminus binds to Golgi membranes. Overexpression of GMAP-210-encoding cDNA induced a dramatic enlargement of the Golgi apparatus and perturbations in the microtubule network. These effects did not occur when a mutant lacking the COOH-terminal domain was expressed. When transfected in fusion with the green fluorescent protein, the NH2-terminal domain associated with the cis-Golgi network whereas the COOH-terminal microtubule-binding domain localized at the centrosome. Altogether these data support the view that GMAP-210 serves to link the cis-Golgi network to the minus ends of centrosome-nucleated microtubules. In addition, this interaction appears essential for ensuring the proper morphology and size of the Golgi apparatus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • COS Cells
  • Centrosome / metabolism*
  • Cytoskeletal Proteins
  • DNA, Complementary / genetics
  • Genes, Reporter
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • Green Fluorescent Proteins
  • HeLa Cells
  • Humans
  • Interphase
  • Luminescent Proteins / analysis
  • Luminescent Proteins / genetics
  • Microscopy, Fluorescence
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / isolation & purification*
  • Microtubule-Associated Proteins / physiology
  • Microtubules / metabolism*
  • Molecular Motor Proteins
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Proteins
  • Paclitaxel / metabolism
  • Paclitaxel / pharmacology
  • Recombinant Fusion Proteins / metabolism
  • Sequence Deletion
  • Transfection
  • Tubulin / metabolism


  • Cytoskeletal Proteins
  • DNA, Complementary
  • Luminescent Proteins
  • Microtubule-Associated Proteins
  • Molecular Motor Proteins
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • TRIP11 protein, human
  • Tubulin
  • Green Fluorescent Proteins
  • Paclitaxel

Associated data

  • GENBANK/Y12490