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

Cross-talk between the two divergent insulin signaling pathways is revealed by the protein kinase B (Akt)-mediated phosphorylation of adapter protein APS on serine 588.

The Journal of biological chemistry - 11 Nov 2005

Katsanakis Kostas D, Pillay Tahir S

Abstract excerpt

The APS adapter protein is recruited to the autophosphorylated kinase domain of the insulin receptor and initiates the phosphatidylinositol 3-kinase (PI3K)-independent pathway of insulin-stimulated glucose transport by recruiting CAP and c-Cbl. In this study, we have identified APS as a novel substrate for protein kinase B/Akt using an antibody that exhibits insulin-dependent immunoreactivity with a...

Read the complete abstract on PubMed

Topics

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

Share to Adipocytes
Share to Amino Acid Motifs

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

Share to Conserved Sequence

Share to Insulin

Share to Phosphatidylinositol 3-Kinases

Share to Phosphoinositide-3 Kinase Inhibitors

Share to Phosphoserine

Share to Proto-Oncogene Proteins c-akt

Source

Identifiers

PMID: 16141217
DOI: 10.1074/jbc.M505959200

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

Cross-talk between the two divergent insulin signaling pathways is revealed by the protein kinase B (Akt)-mediated phosphorylation of adapter protein APS on serine 588.PMID 16141217Read ↗

Role of the juxtamembrane tyrosine in insulin receptor-mediated tyrosine phosphorylation of p60 endogenous substrates.Semantic proximity Read ↗

Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation.Semantic proximity Read ↗

A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.Semantic proximity Read ↗

Structural Basis for Recruitment of the Adaptor Protein APS to the Activated Insulin ReceptorSemantic proximity Read ↗

Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling.Semantic proximity Read ↗

Grb10 and Grb14: enigmatic regulators of insulin action--and more?Semantic proximity Read ↗

A PKB-SPEG signaling nexus links insulin resistance with diabetic cardiomyopathy by regulating calcium homeostasis.Semantic proximity Read ↗

Par14 protein associates with insulin receptor substrate 1 (IRS-1), thereby enhancing insulin-induced IRS-1 phosphorylation and metabolic actions.Semantic proximity Read ↗

Protein kinase B phosphorylation of PIKfyve regulates the trafficking of GLUT4 vesicles.Semantic proximity Read ↗

Positive and negative roles of p85 alpha and p85 beta regulatory subunits of phosphoinositide 3-kinase in insulin signaling.Semantic proximity Read ↗

Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CbetaII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40.Semantic proximity Read ↗

Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo.Semantic proximity Read ↗

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