Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling.
Science
; 278(5335): 103-6, 1997 Oct 03.
Article
em En
| MEDLINE
| ID: mdl-9311911
ABSTRACT
Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the beta subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Delta cell. In vitro Ste5(C177A C180A) bound each component of the MAPK cascade, but not Ste4. Unlike wild-type Ste5, the mutant did not appear to oligomerize; however, when fused to a heterologous dimerization domain (glutathione S-transferase), the chimeric protein restored mating in an ste5Delta cell and an ste4Delta ste5Delta double mutant. Thus, the RING-H2 domain mediates Ste4-Ste5 interaction, which is a prerequisite for Ste5-Ste5 self-association and signaling.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Saccharomyces cerevisiae
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Proteínas Fúngicas
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Transdução de Sinais
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Proteínas de Transporte
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Proteínas de Ligação ao GTP
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Proteínas Heterotriméricas de Ligação ao GTP
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Proteínas de Saccharomyces cerevisiae
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Subunidades beta da Proteína de Ligação ao GTP
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Proteínas Adaptadoras de Transdução de Sinal
Idioma:
En
Ano de publicação:
1997
Tipo de documento:
Article