Two motifs with different function regulate the anterograde transport of the adiponectin receptor 1

Cellular Signalling
Cathleen JuhlAnnette G Beck-Sickinger

Abstract

The anterograde trafficking of GPCR has been described as a tightly controlled process involving specific amino acid sequences that mediate the receptor transport. In this study, we investigated whether the cell surface delivery of the adiponectin receptor 1, a newly identified class of heptahelix receptors different from G protein-coupled receptors, is regulated. Sequential N-terminal deletion revealed that the export of the AdipoR1 from the endoplasmic reticulum (ER) is controlled by distinct parts of the receptor N-terminus. Strong evidence is provided that the ER exit is mediated by two specific sequences, a F(X)(3)F(X)(3)F and a D(X)(3)LL motif. Disruption of these motifs led to a substantial accumulation of the AdipoR1 in the ER. Mutation of similar motifs in the AdipoR1 C-terminus did not result in aberrant receptor localization, suggesting that these motifs are sequence and position specific to the AdipoR1 N-terminus. Further analysis of the regulation mechanism identified an interaction with the chaperone BiP and additionally, strong evidence is provided that both motifs exert different biological function in the AdipoR1 ER export. In conclusion, our data demonstrate that the receptor transport shares similar ER exit m...Continue Reading

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Citations

Feb 5, 2013·Biochemical and Biophysical Research Communications·Sahar KeshvariJonathan P Whitehead
Jan 20, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Matthias KotthoffDietmar Krautwurst

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