2019 journal article

Systematic analysis of F-box proteins reveals a new branch of the yeast mating pathway

JOURNAL OF BIOLOGICAL CHEMISTRY, 294(40), 14717–14731.

author keywords: G protein; mitogen-activated protein kinase (MAPK); yeast; ubiquitin; protein sorting; F-box; fungal mating; pheromone signaling
MeSH headings : Adaptor Proteins, Signal Transducing / genetics; Cell Cycle / genetics; Class III Phosphatidylinositol 3-Kinases / genetics; Endosomes / genetics; F-Box Proteins / chemistry; F-Box Proteins / genetics; GTP-Binding Protein alpha Subunits, Gq-G11 / genetics; GTP-Binding Protein beta Subunits / chemistry; GTP-Binding Protein beta Subunits / genetics; GTP-Binding Protein gamma Subunits / chemistry; GTP-Binding Protein gamma Subunits / genetics; Genes, Mating Type, Fungal / genetics; Morphogenesis / genetics; Pheromones / genetics; Pheromones / metabolism; Saccharomyces cerevisiae / genetics; Saccharomyces cerevisiae / physiology; Saccharomyces cerevisiae Proteins / genetics; Sequence Deletion / genetics; Signal Transduction; Transcription, Genetic; Vacuoles / genetics; Vacuoles / metabolism; cdc42 GTP-Binding Protein / genetics
TL;DR: These findings point to the existence of a new and distinct branch of the pheromone-signaling pathway, one that likely leads to vacuolar engulfment of cytoplasmic proteins and recycling of cellular contents in preparation for mating. (via Semantic Scholar)
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Source: Web Of Science
Added: December 9, 2019

The mating pathway in yeast Saccharomyces cerevisiae has long been used to reveal new mechanisms of signal transduction. The pathway comprises a pheromone receptor, a heterotrimeric G protein, and intracellular effectors of morphogenesis and transcription. Polarized cell growth, in the direction of a potential mating partner, is accomplished by the G-protein βγ subunits and the small G-protein Cdc42. Transcription induction, needed for cell–cell fusion, is mediated by Gβγ and the mitogen-activated protein kinase (MAPK) scaffold protein Ste5. A potential third pathway is initiated by the G-protein α subunit Gpa1. Gpa1 signaling was shown previously to involve the F-box adaptor protein Dia2 and an endosomal effector protein, the phosphatidylinositol 3-kinase Vps34. Vps34 is also required for proper vacuolar sorting and autophagy. Here, using a panel of reporter assays, we demonstrate that mating pheromone stimulates vacuolar targeting of a cytoplasmic reporter protein and that this process depends on Vps34. Through a systematic analysis of F-box deletion mutants, we show that Dia2 is required to sustain pheromone-induced vacuolar targeting. We also found that other F-box proteins selectively regulate morphogenesis (Ydr306, renamed Pfu1) and transcription (Ucc1). These findings point to the existence of a new and distinct branch of the pheromone-signaling pathway, one that likely leads to vacuolar engulfment of cytoplasmic proteins and recycling of cellular contents in preparation for mating.