ArticleProtein science : a publication of the Protein Society2005
Oligomerization of the fifth transmembrane domain from the adenosine A2A receptor.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Purinergic GPCR transmembrane residues involved in ligand recognition and dimerization.Methods in cell biology · 2021Review
- The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking.The Journal of biological chemistry · 2019Article
- Angiotensin II type 1/adenosine AScientific reports · 2017Article
- An Ensemble-Based Protocol for the Computational Prediction of Helix-Helix Interactions in G Protein-Coupled Receptors using Coarse-Grained Molecular Dynamics.Journal of chemical theory and computation · 2017Article
- Article
- A novel PKD2L1 C-terminal domain critical for trimerization and channel function.Scientific reports · 2015Article
- Programmable nanoscaffolds that control ligand display to a G-protein-coupled receptor in membranes to allow dissection of multivalent effects.Journal of the American Chemical Society · 2014Article
- Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain.Journal of virology · 2014Article
- An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization.Protein expression and purification · 2012Article
- Complement factor 5a receptor chimeras reveal the importance of lipid-facing residues in transport competence.The FEBS journal · 2009Article
- Ligand-independent higher-order multimerization of CXCR4, a G-protein-coupled chemokine receptor involved in targeted metastasis.Cancer science · 2009Article
- Trafficking of tachykinin neurokinin 3 receptor to nuclei of neurons in the paraventricular nucleus of the hypothalamus following osmotic challenge.Neuroscience · 2008Article
- Stable interactions between the transmembrane domains of the adenosine A2A receptor.Protein science : a publication of the Protein Society · 2008Article
- The full-length mu-opioid receptor: a conformational study by circular dichroism in trifluoroethanol and membrane-mimetic environments.The Journal of membrane biology · 2008Article
- Oligomerization of neuropeptide Y (NPY) Y2 receptors in CHO cells depends on functional pertussis toxin-sensitive G-proteins.Regulatory peptides · 2007Article
- An unfolding story of helical transmembrane proteins.Biochemistry · 2006Review
- Secretin receptor oligomers form intracellularly during maturation through receptor core domains.Biochemistry · 2006Article
- Redesigning channel-forming peptides: amino acid substitutions that enhance rates of supramolecular self-assembly and raise ion transport activity.Biophysical journal · 2006Article
- Oligomerization of G-protein-coupled receptors: lessons from the yeast Saccharomyces cerevisiae.Eukaryotic cell · 2005Review
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4 authors.
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Abstract
The human adenosine A2A receptor (A(2A)R) belongs to one of the largest family of membrane proteins, the G-protein coupled receptors (GPCRs), characterized by seven transmembrane (TM) helices. Little is known about the determinants of their structures, folding, assembly, activation mechanisms, and oligomeric states. Previous studies in our group showed that peptides corresponding to all seven TM domains form stable helical structures in detergent micelles and lipid vesicles. However, the peptides behave differently; TM5 is the only peptide to have a ratio [theta]222/[theta]208 obtained by circular dichroism (CD) spectroscopy>1. This finding suggested to us that TM5 might self-associate. In the present study, we investigate the unique properties of the TM5 domain. We performed detailed analyses of TM5 peptide behavior in membrane-mimetic environments using CD spectroscopy, fluorescence spectroscopy and Förster resonance energy transfer, and gel electrophoresis. We find that TM5 peptide has the ability to self-associate to form oligomeric structures in various hydrophobic milieus and that these oligomers are highly resistant to temperature and chemical denaturation. We also find that mutation of the full-length A(2A)R at position M193, which is located in the fifth TM domain, noticeably alters A(2A)R monomer: dimer ratio as observed on SDS-PAGE. Our results suggest that parallel association of TM5 dimers may play a role in the known adenosine A2A receptor dimerization. This study represents the first evidence of an individual GPCR transmembrane domain self-association.
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