ArticleThe Biochemical journal1998
Functional rescue of a constitutively desensitized beta2AR through receptor dimerization.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 91 citations in OpenAlex.
- Review
- Critical role of angiotensin II type 2 receptors in the control of mitochondrial and cardiac function in angiotensin II-preconditioned rat hearts.Pflugers Archiv : European journal of physiology · 2018Article
- The G protein-coupled receptor heterodimer network (GPCR-HetNet) and its hub components.International journal of molecular sciences · 2014Article
- Receptor oligomerization: from early evidence to current understanding in class B GPCRs.Frontiers in endocrinology · 2012Article
- Heterodimerization of β2 adrenergic receptor and somatostatin receptor 5: Implications in modulation of signaling pathway.Journal of molecular signaling · 2011Article
- Pharmacology of signaling induced by dopamine D(1)-like receptor activation.Pharmacology & therapeutics · 2010Review
- Molecular mechanisms of the antagonistic action between AT1 and AT2 receptors.Biochemical and biophysical research communications · 2010Article
- Risk factors and myocardial infarction in patients with obstructive sleep apnea: impact of beta2-adrenergic receptor polymorphisms.BMC medicine · 2007Article
- Detection of pairwise residue proximity by covariation analysis for 3D-structure prediction of G-protein-coupled receptors.The protein journal · 2004Article
- Article
- Absence of small conductance K+ channel (SK) activity in apical membranes of thick ascending limb and cortical collecting duct in ROMK (Bartter's) knockout mice.The Journal of biological chemistry · 2002Article
- Chemokine receptor homo- or heterodimerization activates distinct signaling pathways.The EMBO journal · 2001Article
- Genetic polymorphisms of adrenergic receptors.Clinical autonomic research : official journal of the Clinical Autonomic Research Society · 2001Review
- Oligomerization of opioid receptors with beta 2-adrenergic receptors: a role in trafficking and mitogen-activated protein kinase activation.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET).Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Truncated isoforms inhibit [3H]prazosin binding and cellular trafficking of native human alpha1A-adrenoceptors.The Biochemical journal · 1999Article
- Current issues with beta2-adrenoceptor agonists: pharmacology and molecular and cellular mechanisms.Clinical reviews in allergy & immunologyReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have recently demonstrated that wild-type beta2-adrenergic receptors (beta2AR) form homodimers and that disruption of receptor dimerization inhibits signalling via Gs [Hebert, Moffett, Morello, Loisel, Bichet, Barret and Bouvier (1996) J. Biol. Chem. 271, 16384-16392]. Here taking advantage of the altered functional properties of a non-palmitoylated, constitutively desensitized mutant beta2AR (C341Gbeta2AR), we sought to study whether physical interactions between mutant and wild-type beta2AR expressed in Sf9 cells could occur and have functional consequences. Using metabolic labelling with [3H]palmitate and co-immunoprecipitation we demonstrated the existence of heterodimerization between wild-type and C341Gbeta2AR. Furthermore, we show that, in co-expression experiments, wild-type receptors have a dominant positive effect resulting in the functional complementation of C341Gbeta2AR. Indeed, when expressed alone, the mutant C341G receptor displays altered functional characteristics in that (1) the response of the receptor to agonist is reduced as compared to the wild-type receptor and (2) the desensitization of the receptor in response to prolonged exposure to agonist is minimal. In contrast, when C341G and the wild-type beta2AR were expressed together, both the response to agonist and subsequent desensitization (at a constant level of total receptor) were equivalent to the wild-type beta2AR expressed alone. This dominant positive effect was also seen when C341G was co-expressed with a second receptor mutant in which the two protein kinase A phosphorylation sites (S261, 262, 345, 346A beta2AR) were mutated. Taken together these data suggest that intermolecular interactions between receptors may have both functional and structural implications for G-protein-mediated signalling.
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