Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis

• Main Authors: Chien-I Chang, Kimberly A. Schandel, Duane D. Jenness
• Format: Article
• Language: English
• Published: The Company of Biologists 2014-03-01
• Series: Biology Open
• Subjects: G-protein coupled receptors; Receptor oligomers; Ligand-mediated endocytosis
• Online Access: http://bio.biologists.org/content/3/4/297

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.