ArticleInternational journal of molecular sciences2019
IRTKS Promotes Insulin Signaling Transduction through Inhibiting SHIP2 Phosphatase Activity.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Insulin receptor tyrosine kinase substrate in health and disease (Review).Molecular medicine reports · 2025Review
- Heterochromatin formation and remodeling by IRTKS condensates counteract cellular senescence.The EMBO journal · 2024Article
- PHB2 promotes SHIP2 ubiquitination via the E3 ligase NEDD4 to regulate AKT signaling in gastric cancer.Journal of experimental & clinical cancer research : CR · 2024Article
- BAIAP2L1 accelerates breast cancer progression and chemoresistance by activating AKT signaling through binding with ribosomal protein L3.Cancer science · 2023Article
- iTRAQ-Based Proteome Profiling of Differentially Expressed Proteins in Insulin-Resistant Human Hepatocellular Carcinoma.Frontiers in cell and developmental biology · 2022Article
- Upregulated insulin receptor tyrosine kinase substrate promotes the proliferation of colorectal cancer cells via the bFGF/AKT signaling pathway.Gastroenterology report · 2021Article
- Serum Glycoproteomics and Identification of Potential Mechanisms Underlying Alzheimer's Disease.Behavioural neurology · 2021Article
- IQGAP2 Inhibits Migration and Invasion of Gastric Cancer Cells via Elevating SHIP2 Phosphatase Activity.International journal of molecular sciences · 2020Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Insulin signaling is mediated by a highly integrated network that controls glucose metabolism, protein synthesis, cell growth, and differentiation. Our previous work indicates that the insulin receptor tyrosine kinase substrate (IRTKS), also known as BAI1-associated protein 2-like 1 (BAIAP2L1), is a novel regulator of insulin network, but the mechanism has not been fully studied. In this work we reveal that IRTKS co-localizes with Src homology (SH2) containing inositol polyphosphate 5-phosphatase-2 (SHIP2), and the SH3 domain of IRTKS directly binds to SHIP2's catalytic domain INPP5c. IRTKS suppresses SHIP2 phosphatase to convert phosphatidylinositol 3,4,5-triphosphate (PI(3,4,5)P
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