Phosphorylation by Rho kinase regulates CRMP-2 activity in growth cones

Nariko Arimura, Céline Ménager, Yoji Kawano, Takeshi Yoshimura, Saeko Kawabata, Atsushi Hattori, Yuko Fukata, Mutsuki Amano, Yoshio Goshima, Masaki Inagaki, Nobuhiro Morone, Jiro Usukura, Kozo Kaibuchi

研究成果査読

225 被引用数 (Scopus)

抄録

Collapsin response mediator protein 2 (CRMP-2) enhances the advance of growth cones by regulating microtubule assembly and Numb-mediated endocytosis. We previously showed that Rho kinase phosphorylates CRMP-2 during growth cone collapse; however, the roles of phosphorylated CRMP-2 in growth cone collapse remain to be clarified. Here, we report that CRMP-2 phosphorylation by Rho kinase cancels the binding activity to the tubulin dimer, microtubules, or Numb. CRMP-2 binds to actin, but its binding is not affected by phosphorylation. Electron microscopy revealed that CRMP-2 localizes on microtubules, clathrin-coated pits, and actin filaments in dorsal root ganglion neuron growth cones, while phosphorylated CRMP-2 localizes only on actin filaments. The phosphomimic mutant of CRMP-2 has a weakened ability to enhance neurite elongation. Furthermore, ephrin-A5 induces phosphorylation of CRMP-2 via Rho kinase during growth cone collapse. Taken together, these results suggest that Rho kinase phosphorylates CRMP-2, and inactivates the ability of CRMP-2 to promote microtubule assembly and Numb-mediated endocytosis, during growth cone collapse.

本文言語English
ページ(範囲)9973-9984
ページ数12
ジャーナルMolecular and Cellular Biology
25
22
DOI
出版ステータスPublished - 11月 2005
外部発表はい

ASJC Scopus subject areas

  • 分子生物学
  • 細胞生物学

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