Document Type
Article
Publication Date
2014
Published In
Biology Open
Keywords
G-protein coupled receptors, Receptor oligomers, Ligand-mediated 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.
Grant Information
This investigation was supported by Public Health Service research grant GM34719 from the National Institute of General Medical Sciences.
DOI
10.1242/bio.20146866
Creative Commons License
This work is licensed under a Creative Commons Attribution 3.0 License.
Rights
© 2014. Published by The Company of Biologists Ltd.
Recommended Citation
Chang, C.; Schandel, K. A. ; and Jenness, D. D. (2014). Interaction Among Saccharomyces cerevisiae Pheromone Receptors During Endocytosis. Biology Open 2014(3): 297-306. https://doi.org/10.1242/bio.20146866