G Protein-Coupled Receptors Sorting Out Receptors

What are the mechanisms by which different G protein-coupled receptors (GPCRs) are recycled to the cell surface or targeted to the lysosomes for degradation? Whistler et al. (see the Perspective by Gray and Roth) describe the role that one protein, GASP (GPCR-associated sorting protein), plays in the fate of two structurally related opioid GPCRs. The COOH-terminal cytoplasmic domain of the delta opioid receptor but not that of the mu opioid receptor binds to GASP, and this interaction promotes transport to the lysosome. Several other endocytic receptors also interact with GASP, which appears to be a key player in regulating sorting to lysosomes versus recycling after endocytosis.

J. L. Whistler, J. Enquist, A. Marley, J. Fong, F. Gladher, P. Tsuruda, S. R. Murray, M. von Zastrow, Modulation of postendocytic sorting of G protein-coupled receptors, Science 297, 615-620 (2002). [Abstract] [Full Text]

J. A. Gray, B. L. Roth, A last GASP for GPCRs? Science 297, 529-531 (2002). [Summary] [Full Text]

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In Science Magazine

PERSPECTIVES
CELL BIOLOGY:
A Last GASP for GPCRs?

John A. Gray and Bryan L. Roth (26 July 2002)
Science 297 (5581), 529. [DOI: 10.1126/science.1075453]
 |  Summary »  |  Full Text »  |  PDF »

REPORTS
Modulation of Postendocytic Sorting of G Protein-Coupled Receptors

Jennifer L. Whistler, Johan Enquist, Aaron Marley, Jamie Fong, Fredrik Gladher, Pamela Tsuruda, Stephen R. Murray, and Mark von Zastrow (26 July 2002)
Science 297 (5581), 615. [DOI: 10.1126/science.1073308]
 |  Abstract »  |  Full Text »  |  PDF »  |  Supporting Online Material »