Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction.

doi:10.1016/j.jmb.2005.11.012

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Article

Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction.

Journal of molecular biology - 10 Feb 2006

Kwan Jamie J, Warner Neil, Maini Joban, Chan Tung Kelvin W, Zakaria Hoshang, Pawson Tony, Donaldson Logan W

Abstract excerpt

In Saccharomyces cerevisiae, signal transduction through pathways governing mating, osmoregulation, and nitrogen starvation depends upon a direct interaction between the sterile alpha motif (SAM) domains of the Ste11 mitogen-activated protein kinase kinase kinase (MAPKKK) and its regulator Ste50. Previously, we solved the NMR structure of the SAM domain from Ste11 and identified two mutants that diminished...

Topics

Amino Acid Sequence
Amino Acids
Chromatography, Gel
Dimerization
Hydrophobic and Hydrophilic Interactions
Kinetics
MAP Kinase Kinase Kinases
Models, Molecular
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Nuclear Magnetic Resonance, Biomolecular

Protein Binding

Protein Structure, Tertiary

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Sequence Alignment

Sequence Homology, Amino Acid

Surface Plasmon Resonance

Source

Open in PubMed

Identifiers

PMID: 16337230
DOI: 10.1016/j.jmb.2005.11.012

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-16337230-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction.PMID 16337230Read ↗

The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.Semantic proximity Read ↗

Mutations in the SAM domain of STE50 differentially influence the MAPK-mediated pathways for mating, filamentous growth and osmotolerance in Saccharomyces cerevisiae.Semantic proximity Read ↗

Equilibrium unfolding of the dimeric SAM domain of MAPKKK Ste11 from the budding yeast: role of the interfacial residues in structural stability and binding.Semantic proximity Read ↗

The RA domain of Ste50 adaptor protein is required for delivery of Ste11 to the plasma membrane in the filamentous growth signaling pathway of the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Functional characterization of the interaction of Ste50p with Ste11p MAPKKK in Saccharomyces cerevisiae.Semantic proximity Read ↗

The MAPKKK Ste11 regulates vegetative growth through a kinase cascade of shared signaling components.Semantic proximity Read ↗

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Control of MAPK specificity by feedback phosphorylation of shared adaptor protein Ste50.Semantic proximity Read ↗

Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK.Semantic proximity Read ↗

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