Nuclear translocation of Xenopus laevis paxillin

Motoyuki Ogawa, Yoshiki Hiraoka, Sadakazu Aiso

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Paxillin has been recognized as a focal adhesion adapter protein that participates in the integrin-mediated signaling. An earlier study [Ogawa et al. Biochim. Biophys. Acta 1519 (2001) 235] found that frog paxillin was expressed in the kidney epithelial cell line A6 and localized in the nucleus. Here, in this study, we have found that the expression of frog paxillin is up-regulated in the S phase of cell cycle. The protein became phosphorylated on tyrosine when the cells were grown on vitronectin; the tyrosine phosphorylation was not detectable when the cells were cultured on fibronectin, laminin or poly-D-lysine. On the other hand, MAP kinase was revealed to phosphorylate frog paxillin on serine. Both phosphorylation events, namely on tyrosine and serine, were essential for the nuclear translocation of this protein. Our results suggest that the integrin-mediated signaling pathway and the MAP kinase pathway meet at paxillin.

Original languageEnglish
Pages (from-to)676-683
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume304
Issue number4
DOIs
Publication statusPublished - 2003 May 16
Externally publishedYes

Fingerprint

Paxillin
Tyrosine
Phosphorylation
Integrins
Serine
Phosphotransferases
Vitronectin
Proteins
Laminin
Fibronectins
Lysine
Adhesion
Cells

Keywords

  • Cell adhesion
  • Cell cycle
  • Extracellular matrix
  • Nuclear translocation
  • Paxillin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Nuclear translocation of Xenopus laevis paxillin. / Ogawa, Motoyuki; Hiraoka, Yoshiki; Aiso, Sadakazu.

In: Biochemical and Biophysical Research Communications, Vol. 304, No. 4, 16.05.2003, p. 676-683.

Research output: Contribution to journalArticle

Ogawa, Motoyuki ; Hiraoka, Yoshiki ; Aiso, Sadakazu. / Nuclear translocation of Xenopus laevis paxillin. In: Biochemical and Biophysical Research Communications. 2003 ; Vol. 304, No. 4. pp. 676-683.
@article{0b9745bf0406476187cc7f4eb45d3955,
title = "Nuclear translocation of Xenopus laevis paxillin",
abstract = "Paxillin has been recognized as a focal adhesion adapter protein that participates in the integrin-mediated signaling. An earlier study [Ogawa et al. Biochim. Biophys. Acta 1519 (2001) 235] found that frog paxillin was expressed in the kidney epithelial cell line A6 and localized in the nucleus. Here, in this study, we have found that the expression of frog paxillin is up-regulated in the S phase of cell cycle. The protein became phosphorylated on tyrosine when the cells were grown on vitronectin; the tyrosine phosphorylation was not detectable when the cells were cultured on fibronectin, laminin or poly-D-lysine. On the other hand, MAP kinase was revealed to phosphorylate frog paxillin on serine. Both phosphorylation events, namely on tyrosine and serine, were essential for the nuclear translocation of this protein. Our results suggest that the integrin-mediated signaling pathway and the MAP kinase pathway meet at paxillin.",
keywords = "Cell adhesion, Cell cycle, Extracellular matrix, Nuclear translocation, Paxillin",
author = "Motoyuki Ogawa and Yoshiki Hiraoka and Sadakazu Aiso",
year = "2003",
month = "5",
day = "16",
doi = "10.1016/S0006-291X(03)00640-5",
language = "English",
volume = "304",
pages = "676--683",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - Nuclear translocation of Xenopus laevis paxillin

AU - Ogawa, Motoyuki

AU - Hiraoka, Yoshiki

AU - Aiso, Sadakazu

PY - 2003/5/16

Y1 - 2003/5/16

N2 - Paxillin has been recognized as a focal adhesion adapter protein that participates in the integrin-mediated signaling. An earlier study [Ogawa et al. Biochim. Biophys. Acta 1519 (2001) 235] found that frog paxillin was expressed in the kidney epithelial cell line A6 and localized in the nucleus. Here, in this study, we have found that the expression of frog paxillin is up-regulated in the S phase of cell cycle. The protein became phosphorylated on tyrosine when the cells were grown on vitronectin; the tyrosine phosphorylation was not detectable when the cells were cultured on fibronectin, laminin or poly-D-lysine. On the other hand, MAP kinase was revealed to phosphorylate frog paxillin on serine. Both phosphorylation events, namely on tyrosine and serine, were essential for the nuclear translocation of this protein. Our results suggest that the integrin-mediated signaling pathway and the MAP kinase pathway meet at paxillin.

AB - Paxillin has been recognized as a focal adhesion adapter protein that participates in the integrin-mediated signaling. An earlier study [Ogawa et al. Biochim. Biophys. Acta 1519 (2001) 235] found that frog paxillin was expressed in the kidney epithelial cell line A6 and localized in the nucleus. Here, in this study, we have found that the expression of frog paxillin is up-regulated in the S phase of cell cycle. The protein became phosphorylated on tyrosine when the cells were grown on vitronectin; the tyrosine phosphorylation was not detectable when the cells were cultured on fibronectin, laminin or poly-D-lysine. On the other hand, MAP kinase was revealed to phosphorylate frog paxillin on serine. Both phosphorylation events, namely on tyrosine and serine, were essential for the nuclear translocation of this protein. Our results suggest that the integrin-mediated signaling pathway and the MAP kinase pathway meet at paxillin.

KW - Cell adhesion

KW - Cell cycle

KW - Extracellular matrix

KW - Nuclear translocation

KW - Paxillin

UR - http://www.scopus.com/inward/record.url?scp=0037449208&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037449208&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(03)00640-5

DO - 10.1016/S0006-291X(03)00640-5

M3 - Article

VL - 304

SP - 676

EP - 683

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -