Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The cytoplasmic end of transmembrane domain 3 regulates the activity of the Saccharomyces cerevisiae G-protein-coupled alpha-factor receptor.

Genetics - 1 Feb 2002

Parrish William, Eilers Markus, Ying Weiwen, Konopka James B

Abstract excerpt

The binding of alpha-factor to its receptor (Ste2p) activates a G-protein-signaling pathway leading to conjugation of MATa cells of the budding yeast S. cerevisiae. We conducted a genetic screen to identify constitutively activating mutations in the N-terminal region of the alpha-factor receptor that includes transmembrane domains 1-5. This approach identified 12 unique constitutively activating mutations, the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to GTP-Binding Proteins
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Receptors, Mating Factor

Share to Receptors, Peptide

Share to Saccharomyces cerevisiae

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 11861550
DOI: 10.1093/genetics/160.2.429
PMCID: PMC1461982

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The cytoplasmic end of transmembrane domain 3 regulates the activity of the Saccharomyces cerevisiae G-protein-coupled alpha-factor receptor.PMID 11861550Read ↗

A microdomain formed by the extracellular ends of the transmembrane domains promotes activation of the G protein-coupled alpha-factor receptor.Semantic proximity Read ↗

Dominant-negative mutations in the G-protein-coupled alpha-factor receptor map to the extracellular ends of the transmembrane segments.Semantic proximity Read ↗

Aromatic residues at the extracellular ends of transmembrane domains 5 and 6 promote ligand activation of the G protein-coupled alpha-factor receptor.Semantic proximity Read ↗

Interaction between transmembrane domains five and six of the alpha -factor receptor.Semantic proximity Read ↗

The C terminus of the Saccharomyces cerevisiae alpha-factor receptor contributes to the formation of preactivation complexes with its cognate G protein.Semantic proximity Read ↗

The third cytoplasmic loop of a yeast G-protein-coupled receptor controls pathway activation, ligand discrimination, and receptor internalization.Semantic proximity Read ↗

The alpha-factor mating pheromone of Saccharomyces cerevisiae: a model for studying the interaction of peptide hormones and G protein-coupled receptors.Semantic proximity Read ↗

Interacting residues in an activated state of a G protein-coupled receptor.Semantic proximity Read ↗

Substitutions in the hydrophobic core of the alpha-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluyveri alpha-factor and to antagonist.Semantic proximity Read ↗

Disruption of receptor-G protein coupling in yeast promotes the function of an SST2-dependent adaptation pathway.Semantic proximity Read ↗

Mutagenic mapping of helical structures in the transmembrane segments of the yeast alpha-factor receptor.Semantic proximity Read ↗

Mechanisms governing the activation and trafficking of yeast G protein-coupled receptors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.