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Matrix/Integrin Interaction Activates the Mitogen-activated Protein Kinase, p44 and p42
Cell adhesion to extracellular matrix proteins is a dynamic process leading to dramatic changes in the cell phenotype. Integrins are one of the major receptor families that mediate cell-matrix contact. Evidence that integrins can act as signal transducing molecules has accumulated over the past few...
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Published in: | The Journal of biological chemistry 1995-01, Vol.270 (1), p.269 |
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container_start_page | 269 |
container_title | The Journal of biological chemistry |
container_volume | 270 |
creator | Noritsugu Morino Toshihide Mimura Ken Hamasaki Kazuyuki Tobe Kohjiro Ueki Kanako Kikuchi Kazuhiko Takehara Takashi Kadowaki Yoshio Yazaki Yoshihisa Nojima |
description | Cell adhesion to extracellular matrix proteins is a dynamic process leading to dramatic changes in the cell phenotype. Integrins
are one of the major receptor families that mediate cell-matrix contact. Evidence that integrins can act as signal transducing
molecules has accumulated over the past few years. We report here that p44 and p42 mitogen-activated protein (MAP) kinases are rapidly phosphorylated on tyrosine residues upon adhesion of human skin fibroblasts
to fibronectin or upon cross-linking of β1 integrins with antibody. The tyrosine phosphorylation of both kinases is associated
with increased enzymatic activity. Pretreatment of the cells with cytochalasin D, which selectively disrupts the network of
the actin filaments, completely inhibits this adhesion-mediated MAP kinase activation. Thus, our findings indicate that ligation
of β1 integrins induces an increase in both tyrosine phosphorylation and enzymatic activity of p44 and p42 MAP kinases, and that the integrity of the actin cytoskeleton is essential in this process. Since MAP kinase behaves as a
convergence point for diverse receptor-initiated signaling events at the plasma membrane, this serine/threonine kinase plays
a key role and helps to account for the diversity of integrin-dependent cell functions. |
doi_str_mv | 10.1074/jbc.270.1.269 |
format | article |
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are one of the major receptor families that mediate cell-matrix contact. Evidence that integrins can act as signal transducing
molecules has accumulated over the past few years. We report here that p44 and p42 mitogen-activated protein (MAP) kinases are rapidly phosphorylated on tyrosine residues upon adhesion of human skin fibroblasts
to fibronectin or upon cross-linking of β1 integrins with antibody. The tyrosine phosphorylation of both kinases is associated
with increased enzymatic activity. Pretreatment of the cells with cytochalasin D, which selectively disrupts the network of
the actin filaments, completely inhibits this adhesion-mediated MAP kinase activation. Thus, our findings indicate that ligation
of β1 integrins induces an increase in both tyrosine phosphorylation and enzymatic activity of p44 and p42 MAP kinases, and that the integrity of the actin cytoskeleton is essential in this process. Since MAP kinase behaves as a
convergence point for diverse receptor-initiated signaling events at the plasma membrane, this serine/threonine kinase plays
a key role and helps to account for the diversity of integrin-dependent cell functions.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.1.269</identifier><identifier>PMID: 7814385</identifier><language>eng</language><publisher>American Society for Biochemistry and Molecular Biology</publisher><ispartof>The Journal of biological chemistry, 1995-01, Vol.270 (1), p.269</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Noritsugu Morino</creatorcontrib><creatorcontrib>Toshihide Mimura</creatorcontrib><creatorcontrib>Ken Hamasaki</creatorcontrib><creatorcontrib>Kazuyuki Tobe</creatorcontrib><creatorcontrib>Kohjiro Ueki</creatorcontrib><creatorcontrib>Kanako Kikuchi</creatorcontrib><creatorcontrib>Kazuhiko Takehara</creatorcontrib><creatorcontrib>Takashi Kadowaki</creatorcontrib><creatorcontrib>Yoshio Yazaki</creatorcontrib><creatorcontrib>Yoshihisa Nojima</creatorcontrib><title>Matrix/Integrin Interaction Activates the Mitogen-activated Protein Kinase, p44 and p42</title><title>The Journal of biological chemistry</title><description>Cell adhesion to extracellular matrix proteins is a dynamic process leading to dramatic changes in the cell phenotype. Integrins
are one of the major receptor families that mediate cell-matrix contact. Evidence that integrins can act as signal transducing
molecules has accumulated over the past few years. We report here that p44 and p42 mitogen-activated protein (MAP) kinases are rapidly phosphorylated on tyrosine residues upon adhesion of human skin fibroblasts
to fibronectin or upon cross-linking of β1 integrins with antibody. The tyrosine phosphorylation of both kinases is associated
with increased enzymatic activity. Pretreatment of the cells with cytochalasin D, which selectively disrupts the network of
the actin filaments, completely inhibits this adhesion-mediated MAP kinase activation. Thus, our findings indicate that ligation
of β1 integrins induces an increase in both tyrosine phosphorylation and enzymatic activity of p44 and p42 MAP kinases, and that the integrity of the actin cytoskeleton is essential in this process. Since MAP kinase behaves as a
convergence point for diverse receptor-initiated signaling events at the plasma membrane, this serine/threonine kinase plays
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are one of the major receptor families that mediate cell-matrix contact. Evidence that integrins can act as signal transducing
molecules has accumulated over the past few years. We report here that p44 and p42 mitogen-activated protein (MAP) kinases are rapidly phosphorylated on tyrosine residues upon adhesion of human skin fibroblasts
to fibronectin or upon cross-linking of β1 integrins with antibody. The tyrosine phosphorylation of both kinases is associated
with increased enzymatic activity. Pretreatment of the cells with cytochalasin D, which selectively disrupts the network of
the actin filaments, completely inhibits this adhesion-mediated MAP kinase activation. Thus, our findings indicate that ligation
of β1 integrins induces an increase in both tyrosine phosphorylation and enzymatic activity of p44 and p42 MAP kinases, and that the integrity of the actin cytoskeleton is essential in this process. Since MAP kinase behaves as a
convergence point for diverse receptor-initiated signaling events at the plasma membrane, this serine/threonine kinase plays
a key role and helps to account for the diversity of integrin-dependent cell functions.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7814385</pmid><doi>10.1074/jbc.270.1.269</doi><oa>free_for_read</oa></addata></record> |
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title | Matrix/Integrin Interaction Activates the Mitogen-activated Protein Kinase, p44 and p42 |
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