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

Mechanism of SHIP-mediated inhibition of insulin- and platelet-derived growth factor-stimulated mitogen-activated protein kinase activity in 3T3-L1 adipocytes.

Molecular endocrinology (Baltimore, Md.) - 1 Feb 2005

Sharma Prem M, Son Hyun-Shik, Ugi Satoshi, Ricketts William, Olefsky Jerrold M

Abstract excerpt

The Src homology 2-containing 5' inositolphosphatases (SHIP and SHIP2) dephosphorylate 3'-phosphorylated PtdIns on the 5' position, decreasing intracellular levels of PtdIns 3,4,5-P3. In the current study, we investigated the role of SHIP in insulin and platelet-derived growth factor (PDGF) signaling by expressing wild-type (WT) and catalytically inactive SHIPDeltaIP in 3T3-L1 adipocytes, utilizing adenoviral...

Read the complete abstract on PubMed

Topics

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

Share to 3T3-L1 Cells
Share to Adipocytes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epidermal Growth Factor

Share to GRB2 Adaptor Protein

Share to Guanosine Triphosphate

Share to Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases

Share to Platelet-Derived Growth Factor

Share to ras GTPase-Activating Proteins

Source

Identifiers

PMID: 15486046
DOI: 10.1210/me.2004-0096

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

Mechanism of SHIP-mediated inhibition of insulin- and platelet-derived growth factor-stimulated mitogen-activated protein kinase activity in 3T3-L1 adipocytes.PMID 15486046Read ↗

The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells.Semantic proximity Read ↗

Specific tyrosine phosphorylations mediate signal-dependent stimulation of SHIP2 inositol phosphatase activity, while the SH2 domain confers an inhibitory effect to maintain the basal activity.Semantic proximity Read ↗

The role of SHIP in cytokine-induced signaling.Semantic proximity Read ↗

An SH2 domain-containing 5' inositolphosphatase inhibits insulin-induced GLUT4 translocation and growth factor-induced actin filament rearrangement.Semantic proximity Read ↗

BCR/ABL Directly Inhibits Expression of SHIP, an SH2-Containing Polyinositol-5-Phosphatase Involved in the Regulation of HematopoiesisSemantic proximity Read ↗

The role of SHIP in macrophages.Semantic proximity Read ↗

Mechanisms regulating phosphoinositide 3-kinase signalling in insulin-sensitive tissues.Semantic proximity Read ↗

The critical role of Shc in insulin-like growth factor-I-mediated mitogenesis and differentiation in 3T3-L1 preadipocytes.Semantic proximity Read ↗

Tyrosine phosphorylation-dependent and -independent role of Shc in the regulation of IGF-1-induced mitogenesis and glycogen synthesis.Semantic proximity Read ↗

Sp-family of transcription factors regulates human SHIP2 gene expression.Semantic proximity Read ↗

Tyrosine phosphorylation of shc in response to B cell antigen receptor engagement depends on the SHIP inositol phosphatase.Semantic proximity Read ↗

The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor.Semantic proximity Read ↗

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