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ERK signaling promotes cell motility by inducing the localization of myosin 1E to lamellipodial tips.
Tanimura, Susumu; Hashizume, Junya; Arichika, Naoya; Watanabe, Kazushi; Ohyama, Kaname; Takeda, Kohsuke; Kohno, Michiaki.
Afiliación
  • Tanimura S; Department of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan Nagasaki University Research Centre for Genomic Instability and Carcinogenesis, Nagasaki 852-8523, Japan tani1211@nagasaki-u.ac.jp kohnom@nagasaki-u.ac.jp.
  • Hashizume J; Department of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
  • Arichika N; Department of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
  • Watanabe K; Department of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
  • Ohyama K; Department of Pharmacy Practice, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan Nagasaki University Research Centre for Genomic Instability and Carcinogenesis, Nagasaki 852-8523, Japan.
  • Takeda K; Department of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
  • Kohno M; Department of Cell Regulation, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan tani1211@nagasaki-u.ac.jp kohnom@nagasaki-u.ac.jp.
J Cell Biol ; 214(4): 475-89, 2016 08 15.
Article en En | MEDLINE | ID: mdl-27502487
Signaling by extracellular signal-regulated kinase (ERK) plays an essential role in the induction of cell motility, but the precise mechanism underlying such regulation has remained elusive. We recently identified SH3P2 as a negative regulator of cell motility whose function is inhibited by p90 ribosomal S6 kinase (RSK)-mediated phosphorylation downstream of ERK. We here show that myosin 1E (Myo1E) is a binding partner of SH3P2 and that the interaction of the two proteins in the cytosol prevents the localization of Myo1E to the plasma membrane. Serum-induced phosphorylation of SH3P2 at Ser(202) by RSK results in dissociation of Myo1E from SH3P2 in the cytosol and the subsequent localization of Myo1E to the tips of lamellipodia mediated by binding of its TH2 domain to F-actin. This translocation of Myo1E is essential for lamellipodium extension and consequent cell migration. The ERK signaling pathway thus promotes cell motility through regulation of the subcellular localization of Myo1E.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Seudópodos / Movimiento Celular / Sistema de Señalización de MAP Quinasas / Miosina Tipo I Límite: Humans Idioma: En Revista: J Cell Biol Año: 2016 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Seudópodos / Movimiento Celular / Sistema de Señalización de MAP Quinasas / Miosina Tipo I Límite: Humans Idioma: En Revista: J Cell Biol Año: 2016 Tipo del documento: Article Pais de publicación: Estados Unidos