Journal
CELLULAR SIGNALLING
Volume 16, Issue 2, Pages 175-186Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0898-6568(03)00128-1
Keywords
G-protein-coupled receptors; dimerization; heterodimerization; functional complementation; dominant negative; dimerization sites
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Funding
- NIDDK NIH HHS [DK54934] Funding Source: Medline
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Recently, many G-protein-coupled receptors (GPCRs) have been demonstrated to form constitutive dimers consisting of identical or distinct monomeric subunits. The discovery of GPCR dimerization has revealed a new level of molecular cross-talk between signalling molecules and may define a general mechanism that modulates the function of GPCRs under both physiological and pathological conditions. The heterodimerization between distinct GPCRs could be responsible for the generation of pharmacologically defined receptors for which no gene has been identified so far. Elucidating the role of dimerization in the activation processes of GPCRs will lead us to develop novel pharmaceutical agents that allosterically promote activation or inhibition of GPCR signalling. (C) 2003 Elsevier Inc. All rights reserved.
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