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Article

Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast.

Molecular cell - 18 Jun 2004

Marles Jennifer A, Dahesh Samira, Haynes Jennifer, Andrews Brenda J, Davidson Alan R

Abstract excerpt

Protein-protein interactions are required for most cellular functions, yet little is known about the relationship between protein-protein interaction affinity and biological activity. To investigate this issue, we engineered a series of mutants that incrementally reduced the affinity of the yeast...

Topics

Amino Acid Sequence
Binding Sites
Conserved Sequence
MAP Kinase Signaling System
Membrane Proteins
Mitogen-Activated Protein Kinases
Molecular Sequence Data
Mutation
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
src Homology Domains

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Identifiers

PMID: 15200958
DOI: 10.1016/j.molcel.2004.05.024

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-15200958-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast.PMID 15200958Read ↗

Residues neighboring an SH3-binding motif participate in the interaction in vivo.Semantic proximity Read ↗

Interaction Dynamics Determine Signaling and Output Pathway Responses.Semantic proximity Read ↗

Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor.Semantic proximity Read ↗

A docking site determining specificity of Pbs2 MAPKK for Ssk2/Ssk22 MAPKKKs in the yeast HOG pathway.Semantic proximity Read ↗

Analysis of mitogen-activated protein kinase signaling specificity in response to hyperosmotic stress: use of an analog-sensitive HOG1 allele.Semantic proximity Read ↗

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

Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway.Semantic proximity Read ↗

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

Phosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway.Semantic proximity Read ↗

Unique and redundant roles for HOG MAPK pathway components as revealed by whole-genome expression analysis.Semantic proximity Read ↗

Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p.Semantic proximity Read ↗

Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway.Semantic proximity Read ↗

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