| Project/Area Number |
13670025
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General anatomy (including Histology/Embryology)
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| Research Institution | Keio University |
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Principal Investigator |
AISO Sadakazu Keio University, School of Medicine, Department of Anatomy, Professsor, 医学部, 教授 (60138013)
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| Co-Investigator(Kenkyū-buntansha) |
OGAWA Motoyuki Keio University, School of Medicine, Department of Anatomy, Fellow, 医学部, 助手 (90255422)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2002: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2001: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | paxillin / xenopus / cell cycle / paxillin / xenopus / リン酸化 |
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| Research 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, MAPkinase 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.
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