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

A role for autophosphorylation revealed by activated alleles of FUS3, the yeast MAP kinase homolog.

Molecular biology of the cell - 1 Mar 1994

Brill J A, Elion E A, Fink G R

Abstract excerpt

We have isolated dominant gain-of-function (gf) mutations in FUS3, a Saccharomyces cerevisiae mitogen-activated protein (MAP) kinase homolog, that constitutively activate the yeast mating signal transduction pathway and confer hypersensitivity to mating pheromone. Surprisingly, the phenotypes of dominant FUS3gf mutations require the two protein kinases, STE7 and STE11. FUS3gf kinases are hyperphosphorylated in...

Topics

Alleles
Enzyme Activation
Escherichia coli
Fungal Proteins
Genes, Dominant
Genes, Fungal
Mitogen-Activated Protein Kinase Kinases
Mitogen-Activated Protein Kinases
Models, Biological
Mutation
Phosphorylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Kinases

Protein-Tyrosine Kinases

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 8049522
DOI: 10.1091/mbc.5.3.297
PMCID: PMC301038

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8049522-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A role for autophosphorylation revealed by activated alleles of FUS3, the yeast MAP kinase homolog.PMID 8049522Read ↗

Signal transduction in Saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of FUS3 and KSS1.Semantic proximity Read ↗

The MAP kinase Fus3 associates with and phosphorylates the upstream signaling component Ste5.Semantic proximity Read ↗

The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway.Semantic proximity Read ↗

Saccharomyces cerevisiae Ste5 is important for induction and substrate specificity of Fus3 MAP kinase in the pheromone signaling pathway.Semantic proximity Read ↗

Constitutive activation of the Saccharomyces cerevisiae transcriptional regulator Ste12p by mutations at the amino-terminus.Semantic proximity Read ↗

Modulators of MAPK pathway activity during filamentous growth in Saccharomyces cerevisiae.Semantic proximity Read ↗

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.Semantic proximity Read ↗

MAP kinases with distinct inhibitory functions impart signaling specificity during yeast differentiation.Semantic proximity Read ↗

Functional redundancy in the yeast cell cycle: FUS3 and KSS1 have both overlapping and unique functions.Semantic proximity Read ↗

A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission.Semantic proximity Read ↗

The scaffold protein Ste5 directly controls a switch-like mating decision in yeast.Semantic proximity Read ↗

The osmoregulatory pathway represses mating pathway activity in Saccharomyces cerevisiae: isolation of a FUS3 mutant that is insensitive to the repression mechanism.Semantic proximity Read ↗

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