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http://purl.uniprot.org/citations/24719456http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24719456http://www.w3.org/2000/01/rdf-schema#comment"Asymmetric cell growth and division rely on polarized actin cytoskeleton remodeling events, the regulation of which is poorly understood. In budding yeast, formins stimulate the assembly of an organized network of actin cables that direct polarized secretion. Here we show that the Fer/Cip4 homology-Bin amphiphysin Rvs protein Hof1, which has known roles in cytokinesis, also functions during polarized growth by directly controlling the activities of the formin Bnr1. A mutant lacking the C-terminal half of Hof1 displays misoriented and architecturally altered cables, along with impaired secretory vesicle traffic. In vitro, Hof1 inhibits the actin nucleation and elongation activities of Bnr1 without displacing the formin from filament ends. These effects depend on the Src homology 3 domain of Hof1, the formin homology 1 (FH1) domain of Bnr1, and Hof1 dimerization, suggesting a mechanism by which Hof1 "restrains" the otherwise flexible FH1-FH2 apparatus. In vivo, loss of inhibition does not alter actin levels in cables but, instead, cable shape and functionality. Thus Hof1 tunes formins to sculpt the actin cable network."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e14-03-0850"xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Goode B.L."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Yu H.Y."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Eskin J.A."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Garabedian M."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Ydenberg C.A."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Graziano B.R."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Alioto S.L."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/author"Waterman D.P."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/name"Mol Biol Cell"xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/pages"1730-1743"xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/title"The F-BAR protein Hof1 tunes formin activity to sculpt actin cables during polarized growth."xsd:string
http://purl.uniprot.org/citations/24719456http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/24719456http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24719456
http://purl.uniprot.org/citations/24719456http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24719456
http://purl.uniprot.org/uniprot/Q05080#attribution-8B24072A137E70D78A16414F0C2D0BF6http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24719456
http://purl.uniprot.org/uniprot/#_P40450-mappedCitation-24719456http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24719456
http://purl.uniprot.org/uniprot/#_Q05080-mappedCitation-24719456http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24719456
http://purl.uniprot.org/uniprot/P40450http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24719456
http://purl.uniprot.org/uniprot/Q05080http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24719456