ArticleMolecular biology of the cell2006
Akt binds to and phosphorylates phospholipase C-gamma1 in response to epidermal growth factor.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 64 citations in OpenAlex.
- Mammalian PI-Phospholipase C Isozymes: Structural and Functional Insights and Roles in Health and Disease.Medicina (Kaunas, Lithuania) · 2025Review
- PI3K Signaling at the Crossroads of Lipid Metabolism and Cancer.Advances in experimental medicine and biology · 2025Review
- Cell-impermeable staurosporine analog targets extracellular kinases to inhibit HSV and SARS-CoV-2.Communications biology · 2022Article
- Article
- SILAC Phosphoproteomics Reveals Unique Signaling Circuits in CAR-T Cells and the Inhibition of B Cell-Activating Phosphorylation in Target Cells.Journal of proteome research · 2022Article
- EndothelialArteriosclerosis, thrombosis, and vascular biology · 2022Article
- PD-L1 recruits phospholipase C and enhances tumorigenicity of lung tumors harboring mutant forms of EGFR.Cell reports · 2021Article
- Epidermal Growth Factor Stimulates Fatty Acid Synthesis Mainly via PLC-γ1/Akt Signaling Pathway in Dairy Goat Mammary Epithelial Cells.Animals : an open access journal from MDPI · 2020Article
- Comprehensive review of targeted therapy for colorectal cancer.Signal transduction and targeted therapy · 2020Review
- Nuclear Inositides and Inositide-Dependent Signaling Pathways in Myelodysplastic Syndromes.Cells · 2020Review
- Haploinsufficiency of Casitas B-Lineage Lymphoma Augments the Progression of Colon Cancer in the Background of Adenomatous Polyposis Coli Inactivation.The American journal of pathology · 2020Article
- Mechanisms of the Regulation and Dysregulation of Glucagon Secretion.Oxidative medicine and cellular longevity · 2020Review
- Small molecules re-establish neural cell fate of human fibroblasts via autophagy activation.In vitro cellular & developmental biology. Animal · 2019Article
- Review
- Article
- Role of protein kinase N2 (PKN2) in cigarette smoke-mediated oncogenic transformation of oral cells.Journal of cell communication and signaling · 2018Article
- The inhibition of PLCγ1 protects chondrocytes against osteoarthritis, implicating its binding to Akt.Oncotarget · 2018Article
- Receptors That Inhibit Macrophage Activation: Mechanisms and Signals of Regulation and Tolerance.Journal of immunology research · 2018Review
- Phospholipase Cγ1 Mediates Intima Formation Through Akt-Notch1 Signaling Independent of the Phospholipase Activity.Journal of the American Heart Association · 2017Article
- Proteomic Analysis Reveals Autophagy as Pro-Survival Pathway Elicited by Long-Term Exposure with 5-Azacitidine in High-Risk Myelodysplasia.Frontiers in pharmacology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Both phospholipase (PL) C-gamma1 and Akt (protein kinase B; PKB) are signaling proteins that play significant roles in the intracellular signaling mechanism used by receptor tyrosine kinases, including epidermal growth factor (EGF) receptor (EGFR). EGFR activates PLC-gamma1 directly and activates Akt indirectly through phosphatidylinositol 3-kinase (PI3K). Many studies have shown that the PLC-gamma1 pathway and PI3K-Akt pathway interact with each other. However, it is not known whether PLC-gamma1 binds to Akt directly. In this communication, we identified a novel interaction between PLC-gamma1 and Akt. We demonstrated that the interaction is mediated by the binding of PLC-gamma1 Src homology (SH) 3 domain to Akt proline-rich motifs. We also provide a novel model to depict how the interaction between PLC-gamma1 SH3 domain and Akt proline-rich motifs is dependent on EGF stimulation. In this model, phosphorylation of PLC-gamma1 Y783 by EGF causes the conformational change of PLC-gamma1 to allow the interaction of its SH3 domain with Akt proline-rich motifs. Furthermore, we showed that the interaction between PLC-gamma1 and Akt resulted in the phosphorylation of PLC-gamma1 S1248 by Akt. Finally, we showed that the interaction between PLC-gamma1 and Akt enhanced EGF-stimulated cell motility.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.