Maintenance of Y receptor dimers in epithelial cells depends on interaction with G-protein heterotrimers |
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Authors: | Anne-Marie Estes Kathleen McAllen Michael S Parker Renu Sah Trevor Sweatman Edwards A Park Ambikaipakan Balasubramaniam Floyd R Sallee Mary W Walker Steven L Parker |
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Institution: | (1) Department of Pharmacology, UTHSC Memphis, TN, USA;(2) Department of Microbiology, University of Memphis, Memphis, TN, USA;(3) Department of Surgery, University of Cincinnati College of Medicine, Cincinnati, OH, USA;(4) Department of Psychiatry, University of Cincinnati College of Medicine, Cincinnati, OH, USA;(5) Lundbeck Research USA, 215 College Road, Paramus, NJ 07652, USA |
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Abstract: | Treatment of CHO cells expressing human Y receptors (Y1, Y2 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
α 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 α 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:, 2010). |
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