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<title lang=en>Cell-cycle dependent localization of MELK and its new partner RACK1 in epithelial versus mesenchyme-like cells in Xenopus embryo</title>
<creator>Chartrain, Isabelle</creator>
<creator>Le Page, Yann</creator>
<creator>Hatté, Christine</creator>
<creator>Körner, Roman</creator>
<creator>Kubiak, Jacek, </creator>
<creator>Tassan, Jean-Pierre</creator>
<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>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>
<contributor>Max-Planck-Institute for Human Cognitive and Brain Sciences [Leipzig] ; Max Planck Society (GERMANY)</contributor>
<contributor>This work was supported by the Fondation ARC pour la recherche sur le cancer (ARC); Ligue Contre le Cancer; L'Agence Nationale de la Recherche (ANR) (project KinBioFRET); Le Centre National de la Recherche Scientifique (CNRS); and Institut National du Cancer (INCa; to Y.L.P.).</contributor>
<description>International audience</description>
<source>ISSN: 2046-6390</source>
<source>Biology Open</source>
<publisher>Royal Society</publisher>
<identifier>hal-00874053</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00874053</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00874053/document</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00874053/file/Cell-cycle_dependent-accepted.pdf</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00874053</source>
<source>Biology Open, Royal Society, 2013, 2 (10), pp.1037-48. 〈10.1242/bio.20136080〉</source>
<identifier>DOI : 10.1242/bio.20136080</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1242/bio.20136080</relation>
<identifier>PUBMED : 24167714</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/24167714</relation>
<language>en</language>
<subject lang=en>Cell division</subject>
<subject lang=en>Cell polarity</subject>
<subject lang=en>Development</subject>
<subject lang=en>Tight junction</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>Maternal Embryonic Leucine zipper Kinase (MELK) was recently shown to be involved in cell division of Xenopus embryo epithelial cells. The cytokinetic furrow of these cells ingresses asymmetrically and is developmentally regulated. Two subpopulations of xMELK, the mMELK (for "mitotic" xMELK) and iMELK ("interphase" xMELK), which differ in their spatial and temporal regulation, are detected in Xenopus embryo. How cells regulate these two xMELK populations is unknown. In this study we show that, in epithelial cells, xMELK is present at a higher concentration at the apical junctional complex, in contrast to mesenchyme-like cells, which have uniform distribution of cortical MELK. Interestingly, mMELK and iMELK also differ by their requirements towards cell-cell contacts to establish their proper cortical localization both in epithelial and mesenchyme-like cells. Receptor for Activated protein Kinase C (RACK1), which we identified as an xMELK partner, co-localizes with xMELK at the tight junction. Moreover, a truncated RACK1 construct interferes with iMELK localization at cell-cell contacts. Collectively, our results suggest that iMELK and RACK1 are present in the same complex and that RACK1 is involved in the specific recruitment of iMELK at the apical junctional complex in epithelial cells of Xenopus embryos.</description>
<date>2013-07</date>
<contributor>ANR : KinBioFRET, KinBioFRET</contributor>
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