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G-protein coupled receptors, Receptor oligomers, Ligand-mediated endocytosis


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.

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This investigation was supported by Public Health Service research grant GM34719 from the National Institute of General Medical Sciences.



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This work is licensed under a Creative Commons Attribution 3.0 License.


© 2014. Published by The Company of Biologists Ltd.

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