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

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...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Kinetics

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

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Sequence Homology, Amino Acid

Source

Identifiers

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

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

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 ↗

Function of the MAPK scaffold protein, Ste5, requires a cryptic PH domain.Semantic proximity Read ↗

Ste50p is involved in regulating filamentous growth in the yeast Saccharomyces cerevisiae and associates with Ste11p.Semantic proximity Read ↗

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 ↗

Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.Semantic proximity Read ↗

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