The Role of Receptor Oligomerization in Modulating the Expression and Function of Leukocyte Adhesion-g Protein-coupled Receptors.
From: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, United Kingdom.
The Journal of biological chemistry
- Publish Date: Sep 2007
- ISSN: 0021-9258
- Volume: 282
- Issue: 37
- Pages: 27343-53
- Medium: Print
- Language: English
- Citation (JAMA): Davies John Q, Chang Gin-Wen, Yona Simon, et al. The Role of Receptor Oligomerization in Modulating the Expression and Function of Leukocyte Adhesion-g Protein-coupled Receptors.. J. Biol. Chem. Sep 2007;282:27343-53
Abstract
The human leukocyte adhesion-G protein-coupled receptors (GPCRs), the epidermal growth factor (EGF)-TM7 proteins, are shown here to function as homo- and hetero-oligomers. Using cell surface cross-linking, co-immunoprecipitation, and fluorescence resonance energy transfer analysis of EMR2, an EGF-TM7 receptor predominantly expressed in myeloid cells, we demonstrate that it forms dimers in a reaction mediated exclusively by the TM7 moiety. We have also identified a naturally occurring but structurally unstable EMR2 splice variant that acts as a dominant negative modulator by dimerizing with the wild type receptor and down-regulating its expression. Additionally, heterodimerization between closely related EGF-TM7 members is shown to result in the modulation of expression and ligand binding properties of the receptors. These findings suggest that receptor homo- and hetero-oligomerization play a regulatory role in modulating the expression and function of leukocyte adhesion-GPCRs.
Mesh Headings (Keywords): Alternative Splicing, Animals, Antigens, CD, Cells, Cultured, Dimerization, Fluorescence Resonance Energy Transfer, Humans, Leukocytes, Membrane Glycoproteins, Receptors, G-Protein-Coupled
Check for Full Text / PubMed Unique Identifier (PMID): 17620333
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