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

Chunhua Shi, Stephanie C. Kendall, Eric Grote, Susan Kaminskyj, Michèle C. Loewen

Research output: Contribution to journalArticlepeer-review

Abstract

In 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.

Original languageEnglish (US)
Pages (from-to)630-638
Number of pages9
JournalJournal of cellular biochemistry
Volume107
Issue number4
DOIs
StatePublished - Jul 1 2009

Keywords

  • G protein-coupled receptor
  • Mating
  • Mutagenesis
  • Ste2p
  • Yeast

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'N-terminal residues of the yeast pheromone receptor, Ste2p, mediate mating events independently of G1-arrest signaling'. Together they form a unique fingerprint.

Cite this