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dc.contributor.authorFoltman, Magdalena 
dc.contributor.authorFilali-Mouncef Lazcano, Yasmina
dc.contributor.authorCrespo Santiago, Dámaso 
dc.contributor.authorSánchez Díaz, Alberto 
dc.contributor.otherUniversidad de Cantabriaes_ES
dc.date.accessioned2018-07-26T11:20:19Z
dc.date.available2018-07-26T11:20:19Z
dc.date.issued2018-03
dc.identifier.issn1553-7390
dc.identifier.issn1553-7404
dc.identifier.otherBFU2011-23193
dc.identifier.otherBFU2014-58081-P
dc.identifier.urihttp://hdl.handle.net/10902/14206
dc.description.abstractDeposition of additional plasma membrane and cargoes during cytokinesis in eukaryotic cells must be coordinated with actomyosin ring contraction, plasma membrane ingression and extracellular matrix remodelling. The process by which the secretory pathway promotes specific incorporation of key factors into the cytokinetic machinery is poorly understood. Here, we show that cell polarity protein Spa2 interacts with actomyosin ring components during cytokinesis. Spa2 directly binds to cytokinetic factors Cyk3 and Hof1. The lethal effects of deleting the SPA2 gene in the absence of either Cyk3 or Hof1 can be suppressed by expression of the hypermorphic allele of the essential chitin synthase II (Chs2), a transmembrane protein transported on secretory vesicles that makes the primary septum during cytokinesis. Spa2 also interacts directly with the chitin synthase Chs2. Interestingly, artificial incorporation of Chs2 into the cytokinetic machinery allows the localisation of Spa2 at the site of division. In addition, increased Spa2 protein levels promote Chs2 incorporation at the site of division and primary septum formation. Our data indicate that Spa2 is recruited to the cleavage site to co-operate with the secretory vesicle system and particular actomyosin ring components to promote the incorporation of Chs2 into the so-called 'ingression progression complexes' during cytokinesis in budding yeast.es_ES
dc.description.sponsorshipASD was a recipient of a Ramon y Cajal contract (RYC-2010-06156) and received funding from the Cantabria International Campus (http://www.cantabriacampusinternacional.com/Paginas/Cantabria-Campus-de-Excelencia-Internacional.aspx) and via grants BFU2011-23193 and BFU2014-58081-P from the Spanish Ministerio de Economia y Competitividad (co-funded by the European Regional Development Fund) (http:// www.idi.mineco.gob.es/portal/site/MICINN/ menuitem.00d7c011ca2a3753222b7d1001432ea0/?vgnextoid=33881f4368aef110VgnVCM1000001034e20aRCRD) (http://ec.europa.eu/regional_policy/en/funding/erdf/). MF received a Juan de la Cierva contract from the Spanish Ministerio de Economia y Competitividad.es_ES
dc.format.extent32 p.es_ES
dc.language.isoenges_ES
dc.publisherPublic Library of Sciencees_ES
dc.rightsAttribution 4.0 Internationales_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.sourcePLoS Genet. 2018 Mar 30;14(3):e1007299es_ES
dc.titleCell polarity protein Spa2 coordinates Chs2 incorporation at the division site in budding yeastes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherVersionhttps://dx.doi.org/10.1371/journal.pgen.1007299es_ES
dc.rights.accessRightsopenAccesses_ES
dc.identifier.DOI10.1371/journal.pgen.1007299
dc.type.versionpublishedVersiones_ES


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Attribution 4.0 InternationalExcept where otherwise noted, this item's license is described as Attribution 4.0 International