English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/116438
Share/Impact:
Statistics
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Cytokinetic proteins Inn1, Cyk3 and Chs2 form a complex to coordinate plasma membrane ingression and septum formation in budding yeast

AuthorsFoltman, Magdalena ; Molist, Iago; Sacristán, Carlos; Arcones, Irene; Moncalián, Gabriel ; Roncero, Cesar; Sánchez-Díaz, Alberto
Issue Date2014
PublisherFundación Ramón Areces
CitationRamón Areces Foundation International Symposium (2014)
AbstractYeast cells coordinate contraction of the actomyosin ring with primary septum formation, which is produced by the enzyme chitin synthase Chs2. Formation of the septum is precisely an attractive target for therapeutic intervention, as mammalian cells lack the enzymes that synthesise the septum carbohydrates such as chitin. Using the budding yeast Saccharomyces cerevisiae as a model organism, we have described that the actomyosin ring components Inn1 and Cyk3 regulate the catalytic domain of Chs2 during cytokinesis, however the details of such regulation are poorly understood. To try to understand how yeast cells coordinate actomyosin ring contraction, plasma membrane ingression and septum formation we have isolated key actomyosin rings components from yeast cells undergoing cell division. We have identified cytokinetic proteins Inn1, Cyk3 and Chs2, together with other actomyosin ring components including myosin type II, the IQGAP protein Iqg1 and Hof1. We have shown that Inn1 is essential for Chs2 dynamics at the site of division and for Cyk3 to be localized at the bud neck. In addition we have found that Inn1 directly interacts with the catalytic domain of Chs2, and such interaction is not disrupted by point mutations that affect Chs2 activity. Interestingly, we have found that Cyk3 directly interacts with the catalytic domain of Chs2. Together with other groups, we have previously shown that Cyk3 and Inn1 directly interact, and we have now the data indicating that indeed Inn1, Chs2 and Cyk3 form a stable complex. Finally we have determined that the C2 domain of Inn1 is able to increase the chitin activity associated to Chs2 in vitro. Our data clearly demostrate that cytokinetic proteins Inn1, Cyk3 and Chs2 form a complex at the end of mitosis, which plays a key role in coordinating plasma membrane ingression and septum formation.
DescriptionResumen del póster presentado al Ramón Areces Foundation International Symposium: Cell Proliferation and Genome Integrity, celebrado en Santander (España) del 3 al 4 de abril de 2014.
URIhttp://hdl.handle.net/10261/116438
Appears in Collections:(IBBTEC) Comunicaciones congresos
(IBFG) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.