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dc.contributor.authorSanchez-Diaz, Alberto
dc.contributor.authorMarchesi, Vanessa
dc.contributor.authorMurray, Stephen M
dc.contributor.authorJones, Richard C
dc.contributor.authorPereira, Gislene
dc.contributor.authorEdmondson, Ricky D
dc.contributor.authorAllen, Terence D
dc.contributor.authorLabib, Karim
dc.date.accessioned2009-04-23T16:05:07Z
dc.date.available2009-04-23T16:05:07Z
dc.date.issued2008-04
dc.identifier.citationInn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast. 2008, 10 (4):395-406 Nat. Cell Biol.en
dc.identifier.issn1476-4679
dc.identifier.pmid18344988
dc.identifier.doi10.1038/ncb1701
dc.identifier.urihttp://hdl.handle.net/10541/66076
dc.description.abstractBy rapidly depleting each of the essential budding yeast proteins of unknown function, we identified a novel factor that we call Inn1, which associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. We show that Inn1 has a C2 domain at the amino terminus of the protein that is required for ingression of the plasma membrane, whereas the remainder of the protein recruits Inn1 to the actomyosin ring. The lethal effects of deleting the INN1 gene can be suppressed by artificial fusion of the C2 domain to other components of the actomyosin ring, restoring membrane ingression on contraction of the actomyosin ring. Our data indicate that recruitment of the C2 domain of Inn1 to the contractile actomyosin ring is crucial for ingression of the plasma membrane during cytokinesis in budding yeast.
dc.language.isoenen
dc.subject.meshActomyosin
dc.subject.meshAmino Acid Sequence
dc.subject.meshCell Cycle Proteins
dc.subject.meshCell Membrane
dc.subject.meshCytokinesis
dc.subject.meshCytoskeletal Proteins
dc.subject.meshCytoskeleton
dc.subject.meshMitosis
dc.subject.meshModels, Molecular
dc.subject.meshMolecular Sequence Data
dc.subject.meshProtein Conformation
dc.subject.meshProteomics
dc.subject.meshRecombinant Fusion Proteins
dc.subject.meshSaccharomyces Cerevisiae
dc.subject.meshSaccharomyces Cerevisiae Proteins
dc.subject.meshSequence Alignment
dc.titleInn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast.en
dc.typeArticleen
dc.contributor.departmentCancer Research U.K., Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.en
dc.identifier.journalNature Cell Biologyen
html.description.abstractBy rapidly depleting each of the essential budding yeast proteins of unknown function, we identified a novel factor that we call Inn1, which associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. We show that Inn1 has a C2 domain at the amino terminus of the protein that is required for ingression of the plasma membrane, whereas the remainder of the protein recruits Inn1 to the actomyosin ring. The lethal effects of deleting the INN1 gene can be suppressed by artificial fusion of the C2 domain to other components of the actomyosin ring, restoring membrane ingression on contraction of the actomyosin ring. Our data indicate that recruitment of the C2 domain of Inn1 to the contractile actomyosin ring is crucial for ingression of the plasma membrane during cytokinesis in budding yeast.


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