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

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

The Journal of biological chemistry - 30 Mar 2001

Bardwell A J, Flatauer L J, Matsukuma K, Thorner J, Bardwell L

Abstract excerpt

The recognition of mitogen-activated protein kinases (MAPKs) by their upstream activators, MAPK/ERK kinases (MEKs), is crucial for the effective and accurate transmission of many signals. We demonstrated previously that the yeast MAPKs Kss1 and Fus3 bind with high affinity to the N terminus of the MEK Ste7, and proposed that a conserved motif in Ste7, the MAPK-docking site, mediates this interaction. Here we show...

Read the complete abstract on PubMed

Topics

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

Share to Glutathione Transferase
Share to MAP Kinase Signaling System

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

Share to Mitogen-Activated Protein Kinase 1

Share to Mitogen-Activated Protein Kinase Kinases

Share to Mitogen-Activated Protein Kinases

Share to Pheromones

Share to Protein Biosynthesis

Share to Protein Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 11134045
DOI: 10.1074/jbc.M010271200
PMCID: PMC3021106

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

A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission.PMID 11134045Read ↗

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 ↗

Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo.Semantic proximity Read ↗

Control of MAPK signaling specificity by a conserved residue in the MEK-binding domain of the yeast scaffold protein Ste5.Semantic proximity Read ↗

Repression of yeast Ste12 transcription factor by direct binding of unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK.Semantic proximity Read ↗

Dynamics and organization of MAP kinase signal pathways.Semantic proximity Read ↗

Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactorsSemantic proximity Read ↗

Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking.Semantic proximity Read ↗

Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP.Semantic proximity Read ↗

Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactorsSemantic proximity Read ↗

A novel mitogen-activated protein kinase docking site in the N terminus of MEK5alpha organizes the components of the extracellular signal-regulated kinase 5 signaling pathway.Semantic proximity Read ↗

Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction.Semantic proximity Read ↗

PB1 domain-dependent signaling complex is required for extracellular signal-regulated kinase 5 activation.Semantic proximity Read ↗

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