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 phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.

The EMBO journal - 15 Jun 2000

Frödin M, Jensen C J, Merienne K, Gammeltoft S

Abstract excerpt

The 90 kDa ribosomal S6 kinase-2 (RSK2) is a growth factor-stimulated protein kinase with two kinase domains. The C-terminal kinase of RSK2 is activated by ERK-type MAP kinases, leading to autophosphorylation of RSK2 at Ser386 in a hydrophobic motif. The N-terminal kinase is activated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) through phosphorylation of Ser227, and phosphorylates the substrates of...

Read the complete abstract on PubMed

Topics

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

Share to 3-Phosphoinositide-Dependent Protein Kinases
Share to Catalysis

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

Share to Enzyme Activation

Share to Mitogen-Activated Protein Kinases

Share to Protein Serine-Threonine Kinases

Share to Ribosomal Protein S6 Kinases

Share to Ribosomal Protein S6 Kinases, 90-kDa

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 10856237
DOI: 10.1093/emboj/19.12.2924
PMCID: PMC203368

Genes

PDK1

Variants

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 phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.PMID 10856237Read ↗

p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta.Semantic proximity Read ↗

Mutational analysis of ribosomal S6 kinase 2 shows differential regulation of its kinase activity from that of ribosomal S6 kinase 1.Semantic proximity Read ↗

Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.Semantic proximity Read ↗

Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family.Semantic proximity Read ↗

14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity.Semantic proximity Read ↗

Functional Characterization of Human RSK4, a New 90-kDa Ribosomal S6 Kinase, Reveals Constitutive Activation in Most Cell TypesSemantic proximity Read ↗

Bacterial Expression, Purification and In Vitro Phosphorylation of Full-Length Ribosomal S6 Kinase 2 (RSK2).Semantic proximity Read ↗

The Multifaceted Role of S6K1 in Cellular Regulation: Structural Insights, Isoform-Specific Functions, and Therapeutic PotentialSemantic proximity Read ↗

The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling.Semantic proximity Read ↗

Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.Semantic proximity Read ↗

Identification of a regulatory autophosphorylation site in the serine-threonine kinase RIP2.Semantic proximity Read ↗

The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity.Semantic proximity Read ↗

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