ArticleBiochemistry2009
Identification of specific transmembrane residues and ligand-induced interface changes involved in homo-dimer formation of a yeast G protein-coupled receptor.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Early Events in βThe Journal of membrane biology · 2024Article
- Comparison of Experimental Approaches Used to Determine the Structure and Function of the Class D G Protein-Coupled Yeast α-Factor Receptor.Biomolecules · 2022Review
- Article
- Oligomerization of yeast α-factor receptor detected by fluorescent energy transfer between ligands.Biophysical journal · 2021Article
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020Review
- Dynamic roles for the N-terminus of the yeast G protein-coupled receptor Ste2p.Biochimica et biophysica acta. Biomembranes · 2017Article
- Purification of family B G protein-coupled receptors using nanodiscs: Application to human glucagon-like peptide-1 receptor.PloS one · 2017Article
- Variable Dependence of Signaling Output on Agonist Occupancy of Ste2p, a G Protein-coupled Receptor in Yeast.The Journal of biological chemistry · 2016Article
- Evolution of a G protein-coupled receptor response by mutations in regulatory network interactions.Nature communications · 2016Article
- Changes in conformation at the cytoplasmic ends of the fifth and sixth transmembrane helices of a yeast G protein-coupled receptor in response to ligand binding.Biochemistry · 2011Article
- Fungal mating pheromones: choreographing the dating game.Fungal genetics and biology : FG & B · 2011Review
- Regulation of redox signaling by selenoproteins.Biological trace element research · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae alpha-factor pheromone receptor, Ste2p, has been studied as a model for G protein-coupled receptor (GPCR) structure and function. Dimerization has been demonstrated for many GPCRs, although the role(s) of dimerization in receptor function is disputed. Transmembrane domains one (TM1) and four (TM4) of Ste2p were shown previously to play a role in dimerization. In this study, single cysteine substitutions were introduced into a Cys-less Ste2p, and disulfide-mediated dimerization was assessed. Six residues in TM1 (L64 to M69) that had not been previously investigated and 19 residues in TM7 (T278 to A296) of which 15 were not previously investigated were mutated to create 25 single Cys-containing Ste2p molecules. Ste2p mutants V68C in TM1 and nine mutants in TM7 (cysteine substituted into residues 278, 285, 289, and 291 to 296) showed increased dimerization upon addition of an oxidizing agent in comparison to the background dimers formed by the Cys-less receptor. The formation of dimers was decreased for TM7 mutant receptors in the presence of alpha-factor indicating that ligand binding resulted in a conformational change that influenced dimerization. The effect of ligand on dimer formation suggests that dimers are formed in the resting state and the activated state of the receptor by different TM interactions.
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Registered trials
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