Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Rescue of defective G protein–coupled receptor function in vivo by intermolecular cooperation
Aylin C. Hanyaloglub,
Tae H. Jid, and
aDepartment of Physiology, University of Turku, 20520 Turku, Finland; bDepartment of Reproductive Biology, Hammersmith Campus, Imperial College London, London W12 0NN, United Kingdom; cInstitute of Clinical Medicine, National Cheng Kung University Medical College and Hospital, Tainan, 701 Taiwan; and dDepartment of Chemistry, University of Kentucky, Lexington, KY 40506-0055
Edited by Robert J. Lefkowitz, Duke University Medical Center, Durham, NC, and approved October 26, 2009 (received for review June 18, 2009)
G protein–coupled receptors (GPCRs) are ubiquitous mediatorsof signaling of hormones, neurotransmitters, and sensing. Theold dogma is that a one ligand/one receptor complex constitutesthe functional unit of GPCR signaling. However, there is mountingevidence that some GPCRs form dimers or oligomers during theirbiosynthesis, activation, inactivation, and/or internalization.This evidence has been obtained exclusively from cell cultureexperiments, and proof for the physiological significance ofGPCR di/oligomerization in vivo is still missing. Using themouse luteinizing hormone receptor (LHR) as a model GPCR, wedemonstrate that transgenic mice coexpressing binding-deficientand signaling-deficient forms of LHR can reestablish normalLH actions through intermolecular functional complementationof the mutant receptors in the absence of functional wild-typereceptors. These results provide compelling in vivo evidencefor the physiological relevance of intermolecular cooperationin GPCR signaling.
Monomeric Rhodopsin Is Sufficient for Normal Rhodopsin Kinase (GRK1) Phosphorylation and Arrestin-1 Binding.
T. H. Bayburt, S. A. Vishnivetskiy, M. A. McLean, T. Morizumi, C.-c. Huang, J. J. G. Tesmer, O. P. Ernst, S. G. Sligar, and V. V. Gurevich (2011)
J. Biol. Chem.
|Abstract »|Full Text »|PDF »