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CRMP-2 binds to tubulin heterodimers to promote microtubule assembly.

Regulated increase in the formation of microtubule arrays is thought to be important for axonal growth. Collapsin response mediator protein-2 (CRMP-2) is a mammalian homologue of UNC-33, mutations in which result in abnormal axon termination. We recently demonstrated that CRMP-2 is critical for axonal differentiation. Here, we identify two activities of CRMP-2: tubulin-heterodimer binding and the promotion of microtubule assembly. CRMP-2 bound tubulin dimers with higher affinity than it bound microtubules. Association of CRMP-2 with microtubules was enhanced by tubulin polymerization in the presence of CRMP-2. The binding property of CRMP-2 with tubulin was apparently distinct from that of Tau, which preferentially bound microtubules. In neurons, overexpression of CRMP-2 promoted axonal growth and branching. A mutant of CRMP-2, lacking the region responsible for microtubule assembly, inhibited axonal growth and branching in a dominant-negative manner. Taken together, our results suggest that CRMP-2 regulates axonal growth and branching as a partner of the tubulin heterodimer, in a different fashion from traditional MAPs.

Pubmed ID: 12134159

Authors

  • Fukata Y
  • Itoh TJ
  • Kimura T
  • Ménager C
  • Nishimura T
  • Shiromizu T
  • Watanabe H
  • Inagaki N
  • Iwamatsu A
  • Hotani H
  • Kaibuchi K

Journal

Nature cell biology

Publication Data

August 31, 2002

Associated Grants

None

Mesh Terms

  • Animals
  • Axons
  • Cell Line
  • Cercopithecus aethiops
  • Dimerization
  • Fibroblasts
  • Green Fluorescent Proteins
  • Hippocampus
  • In Vitro Techniques
  • Intercellular Signaling Peptides and Proteins
  • Kinetics
  • Luminescent Proteins
  • Microtubules
  • Mutation
  • Nerve Tissue Proteins
  • Neurons
  • Protein Binding
  • Rats
  • Recombinant Fusion Proteins
  • Tubulin
  • Vero Cells