N-Terminal residues of the yeast pheromone receptor, Ste2p, mediate mating events independently of G1-arrest signaling

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DOIResolve DOI: http://doi.org/10.1002/jcb.22129
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TypeArticle
Journal titleJournal of Cellular Biochemistry
Volume107
Issue4
Pages630638; # of pages: 9
SubjectG Protein-coupled receptor; Mating; Mutagenesis; Ste2p; Yeast
AbstractIn Saccharomyces cerevisiae, mechanisms modulating the mating steps following cell cycle arrest are not well characterized. However, the Nterminal domain of Ste2p, a G protein-coupled pheromone receptor, was recently proposed to mediate events at this level. Toward deciphering receptor mechanisms associated with this mating functionality, scanning mutagenesis of targeted regions of the N-terminal domain has been completed. Characterization of ste2 yeast overexpressing Ste2p variants indicated that residues Ile 24 and Ile 29 as well as Pro 15 are critical in mediating mating efficiency. This activity was shown to be independent of Ste2p mediated G1 arrest signaling. Further analysis of Ile 24 and Ile 29 highlight the residues’ solvent accessibility, as well as the importance of the hydrophobic nature of the sites, and in the case of Ile 24 the specific size and shape of the side chain. Mutation of these Ile’s led to arrest of mating after cell contact, but before completion of cell wall degradation. We speculate that these extracellular residues mediate novel receptor interactions with ligand or proteins, leading to stimulation of alternate signaling effector pathways.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Plant Biotechnology Institute
Peer reviewedNo
NPARC number21187432
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Record identifier1de37a15-0553-422c-a692-e2a94929d6b2
Record created2013-01-10
Record modified2016-05-09
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