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

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 Sho1p SH3 domain for its in vivo target, the MAP kinase kinase Pbs2p. We demonstrate a strong linear correlation...

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 Binding Sites

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

Share to Conserved Sequence

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

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

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

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 ↗

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