Journal
AMINO ACIDS
Volume 40, Issue 2, Pages 371-380Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-010-0642-z
Keywords
G-protein coupling receptor; Neuropeptide Y; Receptor dimer; Receptor heteropentamer; Y1 receptor; Y2 receptor; Y4 receptor
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Funding
- U.S. National Institutes of Health [R01 HD-13703]
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Treatment of CHO cells expressing human Y receptors (Y-1, Y-2 or Y4 subtype) with pertussis toxin results in a large decrease in functional receptors, with a preferential loss of heteropentameric assemblies of receptor dimers and G-protein trimers. This occurs in parallel to inactivation of the nucleotide site of Gi alpha subunits, with a half period of about 4 h. The loss could be mainly due to proteolysis at the level of recycling/perinuclear endosomes, and of receptor completion in the ER, since it is reduced by co-treatment with ammonium chloride, an inhibitor of particulate proteinases. Antagonists do not strongly decrease the heteropentameric fraction. These findings indicate that the upkeep of Y receptor dimers in epithelial cell lines depends on the association of receptor oligomers with functional Gi alpha subunits. This interaction could use the juxtamembrane helix 8 in the fourth intracellular domain, and could also be supported by the C-terminal helix of the third intracellular loop, as outlined in the companion review (Parker et al., Amino Acids, doi:10.1007/s00726-010-0616-1, 2010).
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