Dimerization of chemokine receptors and its functional consequences

It became clear over the recent years that most, if not all, G protein-coupled receptors (GPCR) are able to form dimers or higher order oligomers. Chemokine receptors make no exception to this new rule and both homo- and heterodimerization were demonstrated for CC and CXC receptors. Functional analy...

Full description

Saved in:
Bibliographic Details
Published in:Cytokine & growth factor reviews 2005-12, Vol.16 (6), p.611-623
Main Authors: Springael, Jean-Yves, Urizar, Eneko, Parmentier, Marc
Format: Article
Language:English
Subjects:
Animals
Chemokines
Cooperativity
Dimerization
GPCR
HIV Infections - immunology
HIV Infections - metabolism
Humans
Protein Binding
Receptors, Chemokine - physiology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:It became clear over the recent years that most, if not all, G protein-coupled receptors (GPCR) are able to form dimers or higher order oligomers. Chemokine receptors make no exception to this new rule and both homo- and heterodimerization were demonstrated for CC and CXC receptors. Functional analyses demonstrated negative binding cooperativity between the two subunits of a dimer. The consequence is that only one chemokine can bind with high affinity onto a receptor dimer. In the context of receptor activation, this implies that the motions of helical domains triggered by the binding of agonists induce correlated changes in the other protomer. The impact of the chemokine dimerization process in terms of co-receptor function and drug development is discussed.
ISSN:1359-6101
DOI:10.1016/j.cytogfr.2005.05.005