The Dual-Specificity Protein Phosphatase Yvh1p Acts Upstream of the Protein Kinase Mck1p in Promoting Spore Development in Saccharomyces cerevisiae

AUTOR(ES)

Beeser, Alexander E.

FONTE

American Society for Microbiology

RESUMO

Diploid Saccharomyces cerevisiae cells induce YVH1 expression and enter the developmental pathway, leading to sporulation when starved for nitrogen. We show that yvh1 disruption causes a defect in spore maturation; overexpression of MCK1 or IME1 suppresses this yvh1 phenotype. While mck1 mutations are epistatic to those in yvh1 relative to spore maturation, overexpression of MCK1 does not suppress the yvh1 slow-vegetative-growth phenotype. We conclude that (i) Yvh1p functions earlier than Mck1p and Ime1p in the signal transduction cascade that regulates sporulation and is triggered by nitrogen starvation and (ii) the role of Yvh1p in gametogenesis can be genetically distinguished from its role in vegetative growth.

Documentos Relacionados

• The Dual-Specificity Protein Phosphatase Yvh1p Regulates Sporulation, Growth, and Glycogen Accumulation Independently of Catalytic Activity in Saccharomyces cerevisiae via the Cyclic AMP-Dependent Protein Kinase Cascade
• Expression cloning of a human dual-specificity phosphatase.
• Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1
• Overproduction, purification and structure determination of human dual-specificity phosphatase 14
• All-trans-Retinoic Acid Inhibits Jun N-Terminal Kinase by Increasing Dual-Specificity Phosphatase Activity