Structurally unique interaction of RBD-like and PH domains is crucial for yeast pheromone signaling

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DOIResolve DOI: http://doi.org/10.1091/mbc.E12-07-0516
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleMolecular Biology of the Cell
ISSN1059-1524
Volume24
Issue3
Pages409420; # of pages: 12
Subjectmitogen activated protein kinase kinase; pheromone; protein Ste11; protein Ste5; scaffold protein; ubiquitin; unclassified drug; amino acid sequence; article; binding site; cell cycle arrest; cellular distribution; crystal structure; mutational analysis; nonhuman; priority journal; protein binding; protein domain; protein expression; protein folding; protein function; protein motif; protein protein interaction; protein structure; Saccharomyces cerevisiae; Schizosaccharomyces pombe; signal transduction; Adaptor Proteins, Signal Transducing; Amino Acid Substitution; Binding Sites; Genes, Mating Type, Fungal; MAP Kinase Kinase Kinases; Models, Molecular; Mutagenesis, Site-Directed; Peptide Mapping; Pheromones; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Protein Transport; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Signal Transduction
AbstractThe Ste5 protein forms a scaffold that associates and regulates the components of the mitogen-activated protein (MAP) kinase cascade that controls mating-pheromone-mediated signaling in the yeast Saccharomyces cerevisiae. Although it is known that the MEK kinase of the pathway, Ste11, associates with Ste5, details of this interaction have not been established. We identified a Ras-binding-domain-like (RBL) region in the Ste11 protein that is required specifically for the kinase to function in the mating pathway. This module is structurally related to domains in other proteins that mediate Ras-MAP kinase kinase kinase associations; however, this RBL module does not interact with Ras, but instead binds the PH domain of the Ste5 scaffold. Structural and functional studies suggest that the key role of this PH domain is to mediate the Ste5-Ste11 interaction. Overall these two evolutionarily conserved modules interact with each other through a unique interface, and thus in the pheromone pathway the structural context of the RBL domain contribution to kinase activation has been shifted through a change of its interaction partner from Ras to a PH domain. © 2013 Jo et al.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC)
Peer reviewedYes
NPARC number21270599
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Record identifier1cf42cc6-57a0-4184-8b0b-93553c98b856
Record created2014-02-17
Record modified2016-05-09
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