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

Serine 396 of PDK1 is required for maximal PKB activation.

Cellular signalling - 1 Nov 2008

Moon Zoe, Wang Yanping, Aryan Nathan, Mousseau Darrell D, Scheid Michael P

Abstract excerpt

Protein kinase B (PKB; also known as Akt) is important for mediating survival and proliferation signals. Following activation, PKB shuttles to various compartments of the cell, including the nucleus, where it phosphorylates an array of targets. PKB is phosphorylated at T308 by its activator PDK1. PDK1 is normally excluded from the nucleus via a nuclear exclusion sequence (NES), and our previous work suggested...

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 Embryonic Stem Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Extracellular Signal-Regulated MAP Kinases

Share to Forkhead Box Protein O3

Share to Glycogen Synthase Kinase 3

Share to MAP Kinase Kinase Kinases

Share to Recombinases

Share to Ribosomal Protein S6 Kinases

Source

Identifiers

PMID: 18718528
DOI: 10.1016/j.cellsig.2008.07.015

Genes

PDK1
NES

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

Serine 396 of PDK1 is required for maximal PKB activation.PMID 18718528Read ↗

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

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

Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation.Semantic proximity Read ↗

FoxO6 transcriptional activity is regulated by Thr26 and Ser184, independent of nucleo-cytoplasmic shuttling.Semantic proximity Read ↗

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

Nuclear PI3K signaling in cell growth and tumorigenesisSemantic proximity Read ↗

Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a).Semantic proximity Read ↗

Interaction of PDK1 with phosphoinositides is essential for neuronal differentiation but dispensable for neuronal survival.Semantic proximity Read ↗

The N-terminal fragment from caspase-cleaved serine/arginine protein-specific kinase2 (SRPK2) translocates into the nucleus and promotes apoptosis.Semantic proximity Read ↗

Regulation of a third conserved phosphorylation site in SGK1.Semantic proximity Read ↗

Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1.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 ↗

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