Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Characterization of Fus3 localization: active Fus3 localizes in complexes of varying size and specific activity.
Fus3 controls Ty1 transpositional dormancy through the invasive growth MAPK pathway.
MAP kinase dynamics in response to pheromones in budding yeast.
The proteome of Saccharomyces cerevisiae mitochondria.
Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating.
Pheromone-dependent destruction of the Tec1 transcription factor is required for MAP kinase signaling specificity in yeast.
Global analysis of protein phosphorylation in yeast.
The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway.
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling.
Analysis of the yeast kinome reveals a network of regulated protein localization during filamentous growth.
The Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activation.
A global protein kinase and phosphatase interaction network in yeast.
A mechanism for the coordination of proliferation and differentiation by spatial regulation of Fus2p in budding yeast.
Proteome-wide protein interaction measurements of bacterial proteins of unknown function.
Exploitation of latent allostery enables the evolution of new modes of MAP kinase regulation.
ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.
The social and structural architecture of the yeast protein interactome.
Protein-protein interactions in the yeast pheromone response pathway: Ste5p interacts with all members of the MAP kinase cascade.
Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: mating and invasive growth.
Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae.
Reconstitution of a yeast protein kinase cascade in vitro: activation of the yeast MEK homologue STE7 by STE11.
MAP kinase-related FUS3 from S. cerevisiae is activated by STE7 in vitro.
Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7.
Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling.
Posttranslational regulation of Ty1 retrotransposition by mitogen-activated protein kinase Fus3.
Signal transduction in Saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of FUS3 and KSS1.
FUS3 phosphorylates multiple components of the mating signal transduction cascade: evidence for STE12 and FAR1.
Regulation of the mating pheromone and invasive growth responses in yeast by two MAP kinase substrates.
MAP kinases with distinct inhibitory functions impart signaling specificity during yeast differentiation.
Specificity of MAP kinase signaling in yeast differentiation involves transient versus sustained MAPK activation.
Multisite phosphorylation of the Saccharomyces cerevisiae filamentous growth regulator Tec1 is required for its recognition by the E3 ubiquitin ligase adaptor Cdc4 and its subsequent destruction in vivo.
Program-specific distribution of a transcription factor dependent on partner transcription factor and MAPK signaling.
Role of Gα-MAPK interaction in mating of Saccharomyces cerevisiae.
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Gpa1-Fus3 binding contributes to polarity-site guidance during mating.
"Here, we show that the Gα-MAPK interaction can enhance the efficiency of polarity-site alignment between mating partners, particularly under conditions with high Fus3 activity."
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Phosphorylation of Ste4, Ste18, Far1, and Bni1 by Fus3 does not account for the role of the Gpa1-Fus3 interaction in mating.
"Our findings suggest that phosphorylation of Ste4, Ste18, Far1, and Bni1 by Fus3 does not account for the role of the Gpa1–Fus3 interaction in mating."
Falcon deep research report for FUS3
UniProtKB entry P16892 (FUS3_YEAST)
Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p.
Feedback phosphorylation of an RGS protein by MAP kinase in yeast.
SGD gene description for FUS3 (yeast)