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<title lang=en>Identification of ILK as a new partner of the ADAM12 disintegrin and metalloprotease in cell adhesion and survival.</title>
<title lang=en>Identification of ILK as a new partner of the ADAM12 disintegrin and metalloprotease in cell adhesion and survival. : ADAM12-ILK interaction</title>
<creator>Leyme, Anthony</creator>
<creator>Bourd-Boittin, Katia</creator>
<creator>Bonnier, Dominique</creator>
<creator>Falconer, Anaïs</creator>
<creator>Arlot-Bonnemains, Yannick</creator>
<creator>Théret, Nathalie</creator>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Institut de Génétique et Développement de Rennes (IGDR) ; Université de Rennes 1 (UR1) - Centre National de la Recherche Scientifique (CNRS) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Cancer du rein : bases moléculaires de la tumorogenèse ; Institut de Génétique et Développement de Rennes (IGDR) ; Université de Rennes 1 (UR1) - Centre National de la Recherche Scientifique (CNRS) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Université de Rennes 1 (UR1) - Centre National de la Recherche Scientifique (CNRS) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<description>International audience</description>
<source>ISSN: 1059-1524</source>
<source>Molecular Biology of the Cell</source>
<publisher>American Society for Cell Biology</publisher>
<identifier>inserm-00717429</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00717429</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00717429/document</identifier>
<identifier>http://www.hal.inserm.fr/inserm-00717429/file/MBoC_E11-11-0918R-A_LEYME_ET_AL.pdf</identifier>
<source>http://www.hal.inserm.fr/inserm-00717429</source>
<source>Molecular Biology of the Cell, American Society for Cell Biology, 2012, 23 (17), pp.3461-72. 〈10.1091/mbc.E11-11-0918〉</source>
<identifier>PUBMED : 22767580</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/22767580</relation>
<identifier>DOI : 10.1091/mbc.E11-11-0918</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1091/mbc.E11-11-0918</relation>
<language>en</language>
<subject lang=en>ADAM12</subject>
<subject lang=en>ILK</subject>
<subject lang=en>hepatic stellate cells</subject>
<subject>[SDV.BC] Life Sciences [q-bio]/Cellular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Based on its shedding and binding activities, the disintegrin and metalloprotease 12 (ADAM12) has been implicated in cell signaling. Here we investigate the intracellular protein interaction network of the transmembrane ADAM12L variant using an integrative approach. We identify the integrin-linked kinase (ILK) as a new partner for ADAM12L cellular functions. We demonstrate that ADAM12L coimmunoprecipitates with ILK in cells and that its cytoplasmic tail is required for this interaction. In human cultured hepatic stellate cells (HSCs), which express high levels of endogenous ADAM12L and ILK, the two proteins are redistributed to focal adhesions upon stimulation of a β1 integrin-dependent pathway. We show that down-regulation of ADAM12L in HSCs leads to cytoskeletal disorganization and loss of adhesion. Conversely, up-regulation of ADAM12L induces the Akt Ser-473 phosphorylation-dependent survival pathway via stimulation of β1 integrins and activation of phosphoinositide 3-kinase (PI3K). Depletion of ILK inhibits this effect, which is independent of ADAM12L proteolytic activity and involves its cytoplasmic domain. We further demonstrate that overexpression of ADAM12L promotes kinase activity from ILK immunoprecipitates. Our data suggest a new role for ADAM12L in mediating the functional association of ILK with β1 integrin to regulate cell adhesion/survival through a PI3K/Akt signaling pathway.</description>
<date>2012-09</date>
<rights>info:eu-repo/semantics/OpenAccess</rights>
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