The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain

Cell. 1988 Oct 21;55(2):221-34. doi: 10.1016/0092-8674(88)90045-1.

Abstract

The alpha-factor receptor is rapidly hyperphosphorylated on Thr and Ser residues in its hydrophilic C-terminal domain after cells are exposed to pheromone. Mutant receptors in which this domain is altered or removed are biologically active and bind alpha-factor with nearly normal affinity. However, cells expressing the mutant receptors are hypersensitive to pheromone action and appear to be defective in recovery from alpha-factor-induced growth arrest. Mutant receptors with partial C-terminal truncations undergo ligand-induced endocytosis, suggesting that down-regulation of receptor number is not the sole process for adaptation at the receptor level. A mutant receptor lacking the entire C-terminal domain (134 residues) does not display ligand-induced endocytosis. Genetic experiments indicate that the contribution of SST2 function to adaptation does not require the C-terminal domain of the receptor.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Mating Factor
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / analysis
  • Peptides / metabolism*
  • Pheromones / metabolism
  • Receptors, Cell Surface / analysis*
  • Receptors, Mating Factor
  • Receptors, Peptide*
  • Saccharomyces cerevisiae / metabolism*
  • Transcription Factors*

Substances

  • Peptide Fragments
  • Peptides
  • Pheromones
  • Receptors, Cell Surface
  • Receptors, Mating Factor
  • Receptors, Peptide
  • Transcription Factors
  • Mating Factor