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

Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.

The Journal of biological chemistry - 18 Oct 2002

Sato Saori, Fujita Naoya, Tsuruo Takashi

Abstract excerpt

3-Phosphoinositide-dependent protein kinase-1 (PDK1) plays a central role in activating the protein kinase A, G, and C subfamily. In particular, PDK1 plays an important role in regulating the Akt survival pathway by phosphorylating Akt on Thr-308. PDK1 kinase activity was thought to be constitutively active; however, recent reports suggested that its activity is regulated by binding to other proteins, such as...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to 14-3-3 Proteins
Share to 3-Phosphoinositide-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP90 Heat-Shock Proteins

Share to Precipitin Tests

Share to Protein Kinase C

Share to Ribosomal Protein S6 Kinases, 90-kDa

Share to Tyrosine 3-Monooxygenase

Source

Identifiers

PMID: 12177059
DOI: 10.1074/jbc.M205141200

Genes

PDK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.PMID 12177059Read ↗

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

Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 and their role in regulating kinase activity.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 ↗

PDPK1 regulates autophagosome biogenesis by binding to PIK3C3Semantic proximity Read ↗

Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide-dependent kinase-1.Semantic proximity Read ↗

Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways.Semantic proximity Read ↗

14-3-3 Proteins: A Number of Functions for a Numbered ProteinSemantic proximity Read ↗

14-3-3 Proteins: A Number of Functions for a Numbered ProteinSemantic proximity Read ↗

Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway.Semantic proximity Read ↗

Physical association of PDK1 with AKT1 is sufficient for pathway activation independent of membrane localization and phosphatidylinositol 3 kinase.Semantic proximity Read ↗

The C-terminus of Raf-1 acts as a 14-3-3-dependent activation switch.Semantic proximity Read ↗

A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1.Semantic proximity Read ↗

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