Hiroshi Tokuo, M.D., Ph.D.

Hiroshi Tokuo, M.D., Ph.D.

Research Scientist
myosin, cytoskeleton, lamellipodia, filopodia, wound healing 
tokuo@bbri.org

 

Research Summary
During cell migration, the protrusive leading edge plays a key role in directional movement. The leading edge of migrating cells consists of two types of actin cytoskeletal architecture, lamellipodia and filopodia. Our research interest is the mechanism of unconventional myosins in cytoskeletal dynamics, i.e., lamellipodial localization of myosin-I, and filopodia formation by myosin-X. We use a combination of biochemical and molecular techniques, immunocytochemistry, and live cell-imaging techniques. Our goal is to understand a broad range of cell biological processes, including epithelial sheet closure in development, wound healing, neuronal path finding, immune cell function, cell invasion, and metastasis of cancer cells.

 

tl_files/faculty/tukuo_graphic.jpg

 

Selected Publications

  • Tokuo H, Mabuchi K, Ikebe M. The motor activity of myosin-X promotes actin fiber convergence at the cell periphery to initiate filopodia formation. J Cell Biol. 2007;179(2):229-38.
    PMID: 17954606
  • Saeki N, Tokuo H, Ikebe M. BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity. J Biol Chem. 2005;280(11):10128-34.
    PMID: 15644318
  • Ozawa T, Araki N, Yunoue S, Tokuo H, Feng L, Patrakitkomjorn S, Hara T, Ichikawa Y, Matsumoto K, Fujii K, Saya H. The neurofibromatosis type 1 gene product neurofibromin enhances cell motility by regulating actin filament dynamics via the Rho-ROCK-LIMK2-cofilin pathway. J Biol Chem. 2005;280(47):39524-33.
    PMID: 16169856
  • Tokuo H, Ikebe M. Myosin X transports Mena/VASP to the tip of filopodia. Biochem Biophys Res Commun. 2004;319(1):214-20.
    PMID: 15158464
  • Yunoue S, Tokuo H, Fukunaga K, Feng L, Ozawa T, Nishi T, Kikuchi A, Hattori S, Kuratsu J, Saya H, Araki N. Neurofibromatosis type I tumor suppressor neurofibromin regulates neuronal differentiation via its GTPase-activating protein function toward Ras. J Biol Chem. 2003;278(29):26958-69.
    PMID: 12730209
  • Tokuo H, Yunoue S, Feng L, Kimoto M, Tsuji H, Ono T, Saya H, Araki N. Phosphorylation of neurofibromin by cAMP-dependent protein kinase is regulated via a cellular association of N(G),N(G)-dimethylarginine dimethylaminohydrolase. FEBS Lett. 2001;494(1-2):48-53.
    PMID: 11297733

 

PubMed:
Click here for a list of publications (searches the National Library of Medicine's PubMed database.)

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