« Previous AbstractTo transform or not to transform: that is the dilemma in the statistical analysis of plant volatiles    Next AbstractRole of C10-chain in determining aggregation activity of synthetic pheromones for flour beetle Tribolium castaneum (Coleoptera-insecta) »

J Biol Chem

Title:		Systematic analysis of F-box proteins reveals a new branch of the yeast mating pathway
Author(s):		Rangarajan N; Gordy CL; Askew L; Bevill SM; Elston TC; Errede B; Hurst JH; Kelley JB; Sheetz JB; Suzuki SK; Valentin NH; Young E; Dohlman HG;
Address:		"Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599. Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599. Curriculum in Bioinformatics and Computational Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599. Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 hdohlman@med.unc.edu"
Journal Title:		J Biol Chem
Year:		2019
Volume:		20190809
Issue:		40
Page Number:		14717 - 14731
DOI:		10.1074/jbc.RA119.010063
ISSN/ISBN:		1083-351X (Electronic) 0021-9258 (Print) 0021-9258 (Linking)
Abstract:		"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 betagamma subunits and the small G-protein Cdc42. Transcription induction, needed for cell-cell fusion, is mediated by Gbetagamma and the mitogen-activated protein kinase (MAPK) scaffold protein Ste5. A potential third pathway is initiated by the G-protein alpha 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"
Keywords:		"Adaptor Proteins, Signal Transducing/genetics Cell Cycle/genetics Class III Phosphatidylinositol 3-Kinases/*genetics Endosomes/genetics F-Box Proteins/chemistry/*genetics GTP-Binding Protein alpha Subunits, Gq-G11/genetics GTP-Binding Protein beta Subunit;"
Notes:		"MedlineRangarajan, Nambirajan Gordy, Claire L Askew, Lauren Bevill, Samantha M Elston, Timothy C Errede, Beverly Hurst, Jillian H Kelley, Joshua B Sheetz, Joshua B Suzuki, Sara Kimiko Valentin, Natalie H Young, Everett Dohlman, Henrik G eng R01 GM114136/GM/NIGMS NIH HHS/ R35 GM127145/GM/NIGMS NIH HHS/ P30 CA016086/CA/NCI NIH HHS/ T32 GM007040/GM/NIGMS NIH HHS/ K12 GM000678/GM/NIGMS NIH HHS/ R35 GM118105/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't 2019/08/11 J Biol Chem. 2019 Oct 4; 294(40):14717-14731. doi: 10.1074/jbc.RA119.010063. Epub 2019 Aug 9"