title: Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.
abstract: This study investigates endocytosis of Saccharomyces cerevisiae α-factor receptor and the role that receptor oligomerization plays in this process. α-factor receptor contains signal sequences in the cytoplasmic C-terminal domain that are essential for ligand-mediated endocytosis. In an endocytosis complementation assay, we found that oligomeric complexes of the receptor undergo ligand-mediated endocytosis when the α-factor binding site and the endocytosis signal sequences are located in different receptors. Both in vitro and in vivo assays suggested that ligand-induced conformational changes in one Ste2 subunit do not affect neighboring subunits. Therefore, recognition of the endocytosis signal sequence and recognition of the ligand-induced conformational change are likely to be two independent events.
authors.affiliation: Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.
authors.forename: Chien-I
authors.initials: CI
authors.lastname: Chang
authors.forename: Kimberly A
authors.initials: KA
authors.lastname: Schandel
authors.forename: Duane D
authors.initials: DD
authors.lastname: Jenness
keywords: G-protein coupled receptors; Ligand-mediated endocytosis; Receptor oligomers