STE2 Antibody

1. Interaction between Ste2p and Gpa1p takes palce before ligand binding via the Ste2p C-terminal domain and the Gpa1p N-terminal domain. PMID: 28958779
2. yeast pheromone receptor Ste2 forms predominantly tetramers at average expression levels of 2 to 25 molecules per pixel and a mixture of tetramers and octamers at expression levels of 25-100 molecules per pixel. Ste2 is a class D GPCR found in the yeast Saccharomyces cerevisiae of the mating type a, and binds the pheromone a-factor secreted secreted by cells of the mating type a PMID: 27993568
3. The main difference between the Ste2 and Ste3 receptor observed in this work was that while hyperactive mutations were found for Ste3, no gain-of-function mutant for the Ste2 receptor was found. this fi nding is an outcome of the different strategies the two genes have adopted for their expression. PMID: 27150158
4. Results suggest that the G-protein-coupled receptor, Ste2 binds the inhibitory G-protein signaling, Sst2 forming a complex with antagonistic functions. PMID: 28034910
5. Variable Dependence of Signaling Output on Agonist Occupancy of Ste2p, a G Protein-coupled Receptor in Yeast PMID: 27646004
6. results extend previous observations and quantify the contributions of Ste2p variants to mediating cell cycle arrest versus downstream mating functionalities. PMID: 26232403
7. we propose that the N-terminus of Ste2p plays multiple regulatory roles in controlling receptor function. PMID: 26707753
8. A strategy for the identification of stabilized variants of the yeast alpha-factor receptor Ste2p. PMID: 25647246
9. Results show that Ste2 is downregulated by endocytosis, both constitutive and ligand induced and its internalization requires its phosphorylation and ubiquitinylation through the action of alpha arrestins. PMID: 24820415
10. C-terminally trancated forms of Ste2p exert dominant-negative effects. PMID: 22923047
11. structure determination of transmembrane segments of Y4 and the yeast Ste2p G-protein-coupled receptors PMID: 22947943
12. the identification of disulfide bonds that stabilize the active state of the yeast alpha-mating pheromone receptor Ste2p PMID: 22387470
13. C-terminus contains multiple functional domains with differential and interdependent roles in regulating Ste2p function. PMID: 22100461
14. a cryptic polyadenylation site is present inside the coding region of the a-specific STE2 gene, encoding the receptor for the alpha-factor PMID: 21969566
15. study provides new information about role of specific residues of STE2, a GPCR, in signal transduction and how peptide ligand binding activates the receptor PMID: 21728340
16. These results suggest that receptor--agonist interactions, such as those involving Ste2p, involve at least two sites, of which only one is specific for the activated conformation of the receptor. PMID: 21477594
17. Kinetic analysis suggests that alpha-factor associates with its receptor STE2 via a two-stage process consisting of an initial binding event followed by a rearrangement of the ligand-receptor complex. PMID: 15491163
18. Thirty-five different STE2 suppressor mutations were identified by isolating second-site suppressor mutations that restored function to defective receptors carrying either an F204S or Y266C substitution. PMID: 15667221
19. NMR analysis; findings suggest helical subdomains existed in both the transmembrane and cytosolic tail; as the tail participates in down-regulation of Ste2p, helical regions in the tail may play a role in protein-protein interactions in endocytosis PMID: 16128581
20. there is an interaction between specific residues in an active state, but not the resting state, of Ste2p PMID: 16314417
21. that G protein signaling and homologous desensitization are independent cellular processes PMID: 16325780
22. TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of Ste2p PMID: 16478726
23. signal transduction by oligomeric Ste2p receptors appears to be a cooperative process requiring an interaction between functional monomers PMID: 16709573
24. Amiono acid residues of Ste2 that are accessible to the cytoplasmic G-protein are defined and provide an important structural framework for the interpretation of the role of Ste2 residues that function in G-protein activation. PMID: 17176053
25. an interaction between Ste2p and Ste3p has roles in yeast cellular mating PMID: 17369365
26. presence of an alpha-helix in the segment encompassing residues 10-30, which is perturbed around the internal Pro-24 residue PMID: 17449670
27. set the stage for the determination of the 3D structure of these large domains of a G protein-coupled receptor in micelles using high-resolution NMR PMID: 18260136
28. alpha-Factor induced stabilization of the dimeric form and higher order oligomeric forms of the Ste2p receptor. PMID: 18996443
29. Study is the first to report DOPA cross-linking of a peptide hormone to a GPCR and the first to identify a residue-to-residue cross-link between Ste2p and alpha-factor, thereby defining a specific contact point between the bound ligand and its receptor. PMID: 19152328
30. high-resolution NMR study on an 80-residue fragment of Ste2p; data support stable fold for the TM parts of TM1-TM2; NMR structure is consistent with biochemical experiments that identified the ligand-binding site within this region of the receptor PMID: 19383463
31. Results support the conclusion that G protein-coupled receptors, including Ste2, form oligomers and not just dimers, since TM1 and TM4 are too far apart in the class A GPCRs to form contacts in the same dimer moiety. PMID: 19588927
32. The effect of ligand (alpha-factor) on dimer formation of STE2 suggests that dimers are formed in the resting state and the activated state of the receptor by different transmembrane interactions. PMID: 19839649

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KEGG: sce:YFL026W

STRING: 4932.YFL026W