Protein kinase Gin4 negatively regulates flippase function and controls plasma membrane asymmetry.
J Cell Biol
; 208(3): 299-311, 2015 Feb 02.
Article
en En
| MEDLINE
| ID: mdl-25646086
Plasma membrane function requires distinct leaflet lipid compositions. Two of the P-type ATPases (flippases) in yeast, Dnf1 and Dnf2, translocate aminoglycerophospholipids from the outer to the inner leaflet, stimulated via phosphorylation by cortically localized protein kinase Fpk1. By monitoring Fpk1 activity in vivo, we found that Fpk1 was hyperactive in cells lacking Gin4, a protein kinase previously implicated in septin collar assembly. Gin4 colocalized with Fpk1 at the cortical site of future bud emergence and phosphorylated Fpk1 at multiple sites, which we mapped. As judged by biochemical and phenotypic criteria, a mutant (Fpk1(11A)), in which 11 sites were mutated to Ala, was hyperactive, causing increased inward transport of phosphatidylethanolamine. Thus, Gin4 is a negative regulator of Fpk1 and therefore an indirect negative regulator of flippase function. Moreover, we found that decreasing flippase function rescued the growth deficiency of four different cytokinesis mutants, which suggests that the primary function of Gin4 is highly localized control of membrane lipid asymmetry and is necessary for optimal cytokinesis.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Membrana Celular
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Adenosina Trifosfatasas
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Quinasas Ciclina-Dependientes
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Transportadoras de Casetes de Unión a ATP
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Proteínas de Saccharomyces cerevisiae
Idioma:
En
Revista:
J Cell Biol
Año:
2015
Tipo del documento:
Article
Pais de publicación:
Estados Unidos