TY - JOUR
T1 - Nuclear translocation of Xenopus laevis paxillin
AU - Ogawa, Motoyuki
AU - Hiraoka, Yoshiki
AU - Aiso, Sadakazu
N1 - Funding Information:
This work was supported in part by a National Grant-in-Aid for the Establishment of High-Tech Research Center in a Private University from Ministry of Education, Science, Sports and Culture to S.A., and by Grants-in-Aid from the Ministry of Education, Science and Culture to S.A. and M.O.
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
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U2 - 10.1016/S0006-291X(03)00640-5
DO - 10.1016/S0006-291X(03)00640-5
M3 - Article
C2 - 12727207
AN - SCOPUS:0037449208
SN - 0006-291X
VL - 304
SP - 676
EP - 683
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -