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 phosphorylation proximal to its phosphotyrosine binding domain inhibits insulin receptor substrate 1 function and promotes insulin resistance.

Molecular and cellular biology - 1 Nov 2004

Liu Yan-Fang, Herschkovitz Avia, Boura-Halfon Sigalit, Ronen Denise, Paz Keren, Leroith Derek, Zick Yehiel

Abstract excerpt

Ser/Thr phosphorylation of insulin receptor substrate (IRS) proteins negatively modulates insulin signaling. Therefore, the identification of serine sites whose phosphorylation inhibit IRS protein functions is of physiological importance. Here we mutated seven Ser sites located proximal to the phosphotyrosine binding domain of insulin receptor substrate 1 (IRS-1) (S265, S302, S325, S336, S358, S407, and S408)...

Read the complete abstract on PubMed

Topics

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

Share to Adenoviridae
Share to Gene Expression Regulation, Viral

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

Share to Genes, myc

Share to Insulin Receptor Substrate Proteins

Share to Mitogen-Activated Protein Kinases

Share to Phosphoserine

Share to Phosphotyrosine

Share to Proto-Oncogene Proteins c-akt

Source

Open in PubMed Open full text

Identifiers

PMID: 15485932
DOI: 10.1128/MCB.24.21.9668-9681.2004
PMCID: PMC522236

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

Serine phosphorylation proximal to its phosphotyrosine binding domain inhibits insulin receptor substrate 1 function and promotes insulin resistance.PMID 15485932Read ↗

Phosphorylation of Ser357 of rat insulin receptor substrate-1 mediates adverse effects of protein kinase C-delta on insulin action in skeletal muscle cells.Semantic proximity Read ↗

Development and precise characterization of phospho-site-specific antibody of Ser(357) of IRS-1: elimination of cross reactivity with adjacent Ser(358).Semantic proximity Read ↗

Nutrient-dependent and insulin-stimulated phosphorylation of insulin receptor substrate-1 on serine 302 correlates with increased insulin signaling.Semantic proximity Read ↗

Impairment of the IR-IRS-PI3K-AKT signaling pathway in Insulin Resistance: New Insights into Insulin Resistance MechanismsSemantic proximity Read ↗

A single substitution of the insulin receptor kinase inhibits serine autophosphorylation in vitro: evidence for an interaction between the C-terminus and the activation loop.Semantic proximity Read ↗

Regulating insulin signaling and β-cell function through IRS proteinsThis paper is one of a selection of papers published in this Special Issue, entitled Second Messengers and Phosphoproteins—12th International Conference.Semantic proximity Read ↗

PKCdelta-mediated IRS-1 Ser24 phosphorylation negatively regulates IRS-1 function.Semantic proximity Read ↗

Molecular biology of insulin resistance.Semantic proximity Read ↗

Insulin receptor substrate 1 rescues insulin action in CHO cells expressing mutant insulin receptors that lack a juxtamembrane NPXY motif.Semantic proximity Read ↗

Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1.Semantic proximity Read ↗

Prolonged Elimination of Negative Feedback Control Mechanisms Along the Insulin Signaling Pathway Impairs β-Cell Function In Vivo.Semantic proximity Read ↗

Impact of natural IRS-1 mutations on insulin signals: mutations of IRS-1 in the PTB domain and near SH2 protein binding sites result in impaired function at different steps of IRS-1 signaling.Semantic proximity Read ↗

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