ArticleThe Journal of biological chemistry2010
Leukotriene BLT2 receptor monomers activate the G(i2) GTP-binding protein more efficiently than dimers.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 58 citations in OpenAlex.
- Stabilized DNature communications · 2025Article
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure.Nature communications · 2022Article
- A review of non-prostanoid, eicosanoid receptors: expression, characterization, regulation, and mechanism of action.Journal of cell communication and signaling · 2022Review
- Structure of the agonist 12-HHT in its BLT2 receptor-bound state.Scientific reports · 2020Article
- The Endocannabinoid System as a Target in Cancer Diseases: Are We There Yet?Frontiers in pharmacology · 2019Review
- GHSR-D2R heteromerization modulates dopamine signaling through an effect on G protein conformation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Spatial intensity distribution analysis quantifies the extent and regulation of homodimerization of the secretin receptor.The Biochemical journal · 2017Article
- Article
- Differential Contribution of BLT1 and BLT2 to Leukotriene B4-Induced Human NK Cell Cytotoxicity and Migration.Mediators of inflammation · 2015Article
- Large-scale production and protein engineering of G protein-coupled receptors for structural studies.Frontiers in pharmacology · 2015Review
- Amphipols in G protein-coupled receptor pharmacology: what are they good for?The Journal of membrane biology · 2014Review
- Dimers of G-protein coupled receptors as versatile storage and response units.International journal of molecular sciences · 2014Article
- Heterodimerization with Its splice variant blocks the ghrelin receptor 1a in a non-signaling conformation: a study with a purified heterodimer assembled into lipid discs.The Journal of biological chemistry · 2013Article
- The prevalence, maintenance, and relevance of G protein-coupled receptor oligomerization.Molecular pharmacology · 2013Review
- Small angle neutron scattering for the study of solubilised membrane proteins.The European physical journal. E, Soft matter · 2013Review
- Pharmacological modulation of chemokine receptor function.British journal of pharmacology · 2012Review
- High constitutive activity is an intrinsic feature of ghrelin receptor protein: a study with a functional monomeric GHS-R1a receptor reconstituted in lipid discs.The Journal of biological chemistry · 2012Article
- BRET and Time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues.Frontiers in endocrinology · 2012Article
- Light on the structure of thromboxane A₂receptor heterodimers.Cellular and molecular life sciences : CMLS · 2011Article
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Authors and funding
16 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Accumulating evidence indicates that G protein-coupled receptors can assemble as dimers/oligomers but the role of this phenomenon in G protein coupling and signaling is not yet clear. We have used the purified leukotriene B(4) receptor BLT2 as a model to investigate the capacity of receptor monomers and dimers to activate the adenylyl cyclase inhibitory G(i2) protein. For this, we overexpressed the recombinant receptor as inclusion bodies in the Escherichia coli prokaryotic system, using a human alpha(5) integrin as a fusion partner. This strategy allowed the BLT2 as well as several other G protein-coupled receptors from different families to be produced and purified in large amounts. The BLT2 receptor was then successfully refolded to its native state, as measured by high-affinity LTB(4) binding in the presence of the purified G protein G alpha(i2). The receptor dimer, in which the two protomers displayed a well defined parallel orientation as assessed by fluorescence resonance energy transfer, was then separated from the monomer. Using two methods of receptor-catalyzed guanosine 5'-3-O-(thio)triphosphate binding assay, we clearly demonstrated that monomeric BLT2 stimulates the purified G alpha(i2) beta(1) gamma(2) protein more efficiently than the dimer. These data suggest that assembly of two BLT2 protomers into a dimer results in the reduced ability to signal.
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