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Article

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

Cell cycle (Georgetown, Tex.) - 1 Oct 2008

Bayascas Jose R

Abstract excerpt

The 3-phosphoinositide-dependent protein kinase-1 (PDK1) mediates the cellular effect of insulin and growth factors by activating a group of kinases including PKB/Akt, S6K, RSK, SGK and PKC isoforms. PDK1 possesses two regulatory domains namely a Pleckstrin Homology (PH) domain that binds to the phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] second messenger, and a substrate binding site termed the...

Topics

3-Phosphoinositide-Dependent Protein Kinases
Animals
Binding Sites
Insulin Resistance
Mice
Phenotype
Phosphatidylinositol Phosphates
Protein Isoforms
Protein Serine-Threonine Kinases
Protein Structure, Tertiary
Signal Transduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18802401
DOI: 10.4161/cc.7.19.6810

Genes

PDK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways.PMID 18802401Read ↗

The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation.Semantic proximity Read ↗

In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation.Semantic proximity Read ↗

Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates.Semantic proximity Read ↗

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Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1.Semantic proximity Read ↗

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