Regulation of heptaspanning-membrane-receptor function by dimerization and clustering.
G-protein-coupled receptors form homomers and heteromers; agonist-induced conformational changes within interacting receptors of the oligomer modify their pharmacology, signalling and/or trafficking. When these receptors are activated, the oligomers rearrange and cluster and a novel mechanism of receptor-operation regulation by oligomer intercommunication is possible. This intercommunication would be assisted by components of the plasma membrane and by scaffolding proteins. Receptor cross-sensitization, cross-desensitization and novel, integrated receptor responses can then develop between oligomeric receptor complexes of the cluster without direct contact between them. This concept gives a new perspective to the understanding of neurotransmission and neuronal plasticity.
Franco
Rafael
R
Department of Biochemistry and Molecular Biology of the University of Barcelona, Martí Franquès 1, Spain. r.franco@bq.ub.es
Canals
Meritxell
M
Marcellino
Daniel
D
Ferré
Sergi
S
Agnati
Luigi
L
Mallol
Josefa
J
Casadó
Vicent
V
Ciruela
Francisco
F
Fuxe
Kjell
K
Lluis
Carmen
C
Canela
Enric I
EI
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D019281:Dimerization; D006801:Humans; D020836:Protein Structure, Quaternary; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction
D043562:Receptors, G-Protein-Coupled