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<datestamp>2018-01-11</datestamp>
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<title lang=en>Discoidin domain receptor 1 controls linear invadosome formation via a Cdc42-Tuba pathway.</title>
<creator>Juin, Amélie</creator>
<creator>Di Martino, Julie</creator>
<creator>Leitinger, Birgit</creator>
<creator>Henriet, Elodie</creator>
<creator>Gary, Anne-Sophie</creator>
<creator>Paysan, Lisa</creator>
<creator>Bomo, Jeremy</creator>
<creator>Baffet, Georges</creator>
<creator>Gauthier-Rouvière, Cécile</creator>
<creator>Rosenbaum, Jean</creator>
<creator>Moreau, Violaine</creator>
<creator>Saltel, Frédéric</creator>
<contributor>Physiopathologie du cancer du foie ; Université Bordeaux Segalen - Bordeaux 2 - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<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>Centre de recherches de biochimie macromoléculaire (CRBM) ; Université Montpellier 1 (UM1) - Université Montpellier 2 - Sciences et Techniques (UM2) - Université de Montpellier (UM) - Centre National de la Recherche Scientifique (CNRS)</contributor>
<description>International audience</description>
<source>ISSN: 0021-9525</source>
<source>EISSN: 1540-8140</source>
<source>Journal of Cell Biology</source>
<publisher>Rockefeller University Press</publisher>
<identifier>hal-01118481</identifier>
<identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01118481</identifier>
<source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01118481</source>
<source>Journal of Cell Biology, Rockefeller University Press, 2014, 207 (4), pp.517-33. 〈10.1083/jcb.201404079〉</source>
<identifier>PUBMED : 25422375</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/25422375</relation>
<identifier>DOI : 10.1083/jcb.201404079</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1083/jcb.201404079</relation>
<identifier>PUBMEDCENTRAL : PMC4242841</identifier>
<language>en</language>
<subject>[SDV] Life Sciences [q-bio]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Accumulation of type I collagen fibrils in tumors is associated with an increased risk of metastasis. Invadosomes are F-actin structures able to degrade the extracellular matrix. We previously found that collagen I fibrils induced the formation of peculiar linear invadosomes in an unexpected integrin-independent manner. Here, we show that Discoidin Domain Receptor 1 (DDR1), a collagen receptor overexpressed in cancer, colocalizes with linear invadosomes in tumor cells and is required for their formation and matrix degradation ability. Unexpectedly, DDR1 kinase activity is not required for invadosome formation or activity, nor is Src tyrosine kinase. We show that the RhoGTPase Cdc42 is activated on collagen in a DDR1-dependent manner. Cdc42 and its specific guanine nucleotide-exchange factor (GEF), Tuba, localize to linear invadosomes, and both are required for linear invadosome formation. Finally, DDR1 depletion blocked cell invasion in a collagen gel. Altogether, our data uncover an important role for DDR1, acting through Tuba and Cdc42, in proteolysis-based cell invasion in a collagen-rich environment.</description>
<date>2014-11-24</date>
</dc>
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