| Title: | The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain |
| Author(s): | Reneke JE; Blumer KJ; Courchesne WE; Thorner J; |
| Address: | "Department of Biochemistry University of California, Berkeley 94720" |
| DOI: | 10.1016/0092-8674(88)90045-1 |
| ISSN/ISBN: | 0092-8674 (Print) 0092-8674 (Linking) |
| 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" |
| Keywords: | "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;" |
| Notes: | "MedlineReneke, J E Blumer, K J Courchesne, W E Thorner, J eng GM07127/GM/NIGMS NIH HHS/ GM21841/GM/NIGMS NIH HHS/ 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. 1988/10/21 Cell. 1988 Oct 21; 55(2):221-34. doi: 10.1016/0092-8674(88)90045-1" |
