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Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology

Author

Listed:
  • Yong Kim

    (The Rockefeller University)

  • Jee Young Sung

    (The Rockefeller University)

  • Ilaria Ceglia

    (The Rockefeller University)

  • Ko-Woon Lee

    (The Rockefeller University)

  • Jung-Hyuck Ahn

    (The Rockefeller University)

  • Jonathan M. Halford

    (The Rockefeller University)

  • Amie M. Kim

    (The Rockefeller University)

  • Seung P. Kwak

    (Wyeth Research)

  • Jong Bae Park

    (Pohang University of Science and Technology)

  • Sung Ho Ryu

    (Pohang University of Science and Technology)

  • Annette Schenck

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP)

  • Barbara Bardoni

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP)

  • John D. Scott

    (Howard Hughes Medical Institute, Vollum Institute)

  • Angus C. Nairn

    (The Rockefeller University
    Yale University School of Medicine)

  • Paul Greengard

    (The Rockefeller University)

Abstract

WAVE1—the Wiskott–Aldrich syndrome protein (WASP)-family verprolin homologous protein 1—is a key regulator of actin-dependent morphological processes1 in mammals, through its ability to activate the actin-related protein (Arp2/3) complex. Here we show that WAVE1 is phosphorylated at multiple sites by cyclin-dependent kinase 5 (Cdk5) both in vitro and in intact mouse neurons. Phosphorylation of WAVE1 by Cdk5 inhibits its ability to regulate Arp2/3 complex-dependent actin polymerization. Loss of WAVE1 function in vivo or in cultured neurons results in a decrease in mature dendritic spines. Expression of a dephosphorylation-mimic mutant of WAVE1 reverses this loss of WAVE1 function in spine morphology, but expression of a phosphorylation-mimic mutant does not. Cyclic AMP (cAMP) signalling reduces phosphorylation of the Cdk5 sites in WAVE1, and increases spine density in a WAVE1-dependent manner. Our data suggest that phosphorylation/dephosphorylation of WAVE1 in neurons has an important role in the formation of the filamentous actin cytoskeleton, and thus in the regulation of dendritic spine morphology.

Suggested Citation

  • Yong Kim & Jee Young Sung & Ilaria Ceglia & Ko-Woon Lee & Jung-Hyuck Ahn & Jonathan M. Halford & Amie M. Kim & Seung P. Kwak & Jong Bae Park & Sung Ho Ryu & Annette Schenck & Barbara Bardoni & John D., 2006. "Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology," Nature, Nature, vol. 442(7104), pages 814-817, August.
    • Handle: RePEc:nat:nature:v:442:y:2006:i:7104:d:10.1038_nature04976
    DOI: 10.1038/nature04976
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    Cited by:

    1. Weiji Weng & Xiaokun Gu & Yang Yang & Qiao Zhang & Qi Deng & Jie Zhou & Jinke Cheng & Michael X. Zhu & Junfeng Feng & Ou Huang & Yong Li, 2023. "N-terminal α-amino SUMOylation of cofilin-1 is critical for its regulation of actin depolymerization," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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