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Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling

Author

Listed:
  • Fumio Nakamura

    (Yokohama City University Graduate School of Medicine)

  • Kosuke Kumeta

    (Yokohama City University Graduate School of Medicine)

  • Tomonobu Hida

    (Yokohama City University Graduate School of Medicine)

  • Toshinari Isono

    (Yokohama City University Graduate School of Medicine
    Yokohama National University)

  • Yuichi Nakayama

    (Yokohama City University Graduate School of Medicine)

  • Emiko Kuramata-Matsuoka

    (Yokohama City University Graduate School of Medicine)

  • Naoya Yamashita

    (Yokohama City University Graduate School of Medicine)

  • Yutaka Uchida

    (Yokohama City University Graduate School of Medicine)

  • Ken-ichi Ogura

    (Yokohama City University Graduate School of Medicine)

  • Keiko Gengyo-Ando

    (Tokyo Women’s Medical University School of Medicine)

  • Shohei Mitani

    (Tokyo Women’s Medical University School of Medicine)

  • Toshio Ogino

    (Yokohama National University)

  • Yoshio Goshima

    (Yokohama City University Graduate School of Medicine)

Abstract

Reorganization of the actin cytoskeleton is an early cellular response to various extracellular signals. Sema3A, a repulsive axon guidance molecule, induces the reorganization of actin cytoskeleton in the growth cones. Collapsin response mediator protein 1 (CRMP1) mediates the intracellular Sema3A signalling through its Ser522 phosphorylation. Here we show that UNC-33, CRMP1 C. elegans homologue, interacts with FLN-1, an actin-binding Filamin-A orthologue. In nematodes, this interaction participates in the projection of DD/VD motor neurons. CRMP1 binds both the actin-binding domain and the last immunoglobulin-like repeat of Filamin-A. The alanine mutants of Filamin-A or CRMP1 in their interacting residues suppress the Sema3A repulsion in neurons. Conversely, a phosphor-mimicking mutant CRMP1(Ser522Asp) enhances the Sema3A response. Atomic-force microscopy analysis reveals that the V-shaped Filamin-A changes to a condensed form with CRMP1(Ser522Asp). CRMP1(Ser522Asp) weakens the F-actin gelation crosslinked by Filamin-A. Thus, phosphorylated CRMP1 may remove Filamin-A from the actin cytoskeleton to facilitate its remodelling.

Suggested Citation

  • Fumio Nakamura & Kosuke Kumeta & Tomonobu Hida & Toshinari Isono & Yuichi Nakayama & Emiko Kuramata-Matsuoka & Naoya Yamashita & Yutaka Uchida & Ken-ichi Ogura & Keiko Gengyo-Ando & Shohei Mitani & To, 2014. "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling," Nature Communications, Nature, vol. 5(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6325
    DOI: 10.1038/ncomms6325
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