TY - JOUR
T1 - The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain
AU - Reneke, Johanna E.
AU - Blumer, Kendall J.
AU - Courchesne, William E.
AU - Thorner, Jeremy
N1 - Funding Information:
This work was supported by a National Science Foundation Predoctoral Fellowship and by the National Institutes of Health Predoctoral Traineeship GMO7l27to J. E. R., by American Cancer Society Postdoctoral Fellowship PF2632 to K. J. B., by Damon Runyon-Walter Win-chell Cancer Research Fund Postdoctoral Fellowship DRG836, and by Senior Postdoctoral Fellowship S15-87 from the California Division of the American Cancer Society to W. E. C., and by National Institutes of Health Research Grant GM21841 to J. T The authors wish to thank the following individuals for the generous gift of research materials, for helpful advice, or for the communication of results prior to publication: Nancy Kleckner, George Sprague, Duane Jenness, Vivian MacKay, Malcolm Whiteway, Lorraine Marsh, Ira Herskowitz, and Janet Kurjan. We also thank Philip J. Gotwals for construction of plasmid pJGsst7.
PY - 1988/10/21
Y1 - 1988/10/21
N2 - The α-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 α-factor with nearly normal affinity. However, cells expressing the mutant receptors are hypersensitive to pheromone action and appear to be defective in recovery from α-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.
AB - The α-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 α-factor with nearly normal affinity. However, cells expressing the mutant receptors are hypersensitive to pheromone action and appear to be defective in recovery from α-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.
UR - http://www.scopus.com/inward/record.url?scp=0024294018&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(88)90045-1
DO - 10.1016/0092-8674(88)90045-1
M3 - Article
C2 - 2844413
AN - SCOPUS:0024294018
SN - 0092-8674
VL - 55
SP - 221
EP - 234
JO - Cell
JF - Cell
IS - 2
ER -