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<OAI-PMH schemaLocation=http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd> <responseDate>2018-01-15T18:33:22Z</responseDate> <request identifier=oai:HAL:hal-01063933v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request> <GetRecord> <record> <header> <identifier>oai:HAL:hal-01063933v1</identifier> <datestamp>2017-12-21</datestamp> <setSpec>type:ART</setSpec> <setSpec>subject:sdv</setSpec> <setSpec>collection:IRSET</setSpec> <setSpec>collection:UNIV-RENNES1</setSpec> <setSpec>collection:UNIV-AG</setSpec> <setSpec>collection:IFR140</setSpec> <setSpec>collection:IRSET-TREC</setSpec> <setSpec>collection:BIOSIT</setSpec> <setSpec>collection:UR1-UFR-SVE</setSpec> <setSpec>collection:STATS-UR1</setSpec> <setSpec>collection:UR1-HAL</setSpec> <setSpec>collection:EHESP</setSpec> <setSpec>collection:USPC</setSpec> <setSpec>collection:UR1-SDV</setSpec> <setSpec>collection:IRSET-6</setSpec> <setSpec>collection:UNIV-ANGERS</setSpec> </header> <metadata><dc> <publisher>HAL CCSD</publisher> <title lang=en>The actin/MKL1 signalling pathway influences cell growth and gene expression through large-scale chromatin reorganization and histone post-translational modifications</title> <creator>Flouriot, Gilles</creator> <creator>Huet, Guillaume</creator> <creator>Demay, Florence</creator> <creator>Pakdel, Farzad</creator> <creator>Boujrad, Noureddine</creator> <creator>Michel, Denis</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>TREC : Transcription, Environment and Cancer ; 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 ) - 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> <description>International audience</description> <source>The Biochemical Journal</source> <identifier>hal-01063933</identifier> <identifier>https://hal.archives-ouvertes.fr/hal-01063933</identifier> <source>https://hal.archives-ouvertes.fr/hal-01063933</source> <source>The Biochemical Journal, 2014, 461 (2), pp.257--268. 〈10.1042/BJ20131240〉</source> <identifier>DOI : 10.1042/BJ20131240</identifier> <relation>info:eu-repo/semantics/altIdentifier/doi/10.1042/BJ20131240</relation> <identifier>PUBMED : 24762104</identifier> <relation>info:eu-repo/semantics/altIdentifier/pmid/24762104</relation> <language>en</language> <subject lang=en>Acetylation</subject> <subject lang=en>Actins</subject> <subject lang=en>Cell Line</subject> <subject lang=en>Tumor</subject> <subject lang=en>Cell Proliferation</subject> <subject lang=en>Chromatin</subject> <subject lang=en>Chromatin Assembly and Disassembly</subject> <subject lang=en>DNA-Binding Proteins</subject> <subject lang=en>Epithelial-Mesenchymal Transition</subject> <subject lang=en>Gene Expression</subject> <subject lang=en>Histones</subject> <subject lang=en>Humans</subject> <subject lang=en>Methylation</subject> <subject lang=en>Oncogene Proteins</subject> <subject lang=en>Fusion</subject> <subject lang=en>Protein Processing</subject> <subject lang=en>Post-Translational</subject> <subject lang=en>Signal Transduction</subject> <subject>[SDV] Life Sciences [q-bio]</subject> <type>info:eu-repo/semantics/article</type> <type>Journal articles</type> <description lang=en>In addition to soluble factors, mechanical constraints and extracellular matrix stiffness are important regulators of cell fate that are mediated by cytoskeletal modifications. The EMT (epithelial-mesenchymal transition) that occurs during normal development and malignant progression is a typical example of the phenotypic switch associated with profound actin remodelling and changes in gene expression. For instance, actin dynamics control motile cell functions in EMT, in part, through regulating the subcellular localization of the myocardin-related transcription factor MKL1 (megakaryoblastic leukaemia translocation 1), a co-activator of SRF (serum-responsive factor). In the present paper, we show that MKL1 participates also to the control of the cellular switch between growth and quiescence. Experimental disconnection between MKL1 and G-actin (globular actin), by using an MKL1 mutant or enhancing the F (filamentous)-/G-actin ratio, generates a widely open chromatin state and a global increase in biosynthetic activity, classically associated with cell growth. Conversely, G-actin accumulation favours nuclear condensation and cell quiescence. These large-scale chromatin changes rely upon extensive histone modifications, exemplified by that of H3K9 (H3 Lys9) shifting from trimethylation, a heterochromatin mark, to acetylation, a mark of euchromatin. The present study provides the first evidence for a global reversible hetero/euchromatinization phenomenon triggered by the actin/MKL1 signalling pathway.</description> <date>2014</date> </dc> </metadata> </record> </GetRecord> </OAI-PMH>