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- W2912649349 endingPage "e3000133" @default.
- W2912649349 startingPage "e3000133" @default.
- W2912649349 abstract "How multiple receptor tyrosine kinases coordinate cell fate determination is yet to be elucidated. We show here that the receptor for platelet-derived growth factor (PDGF) signaling recruits the p85 subunit of Phosphoinositide 3-kinase (PI3K) to regulate mammalian lens development. Activation of PI3K signaling not only prevents B-cell lymphoma 2 (BCL2)-Associated X (Bax)- and BCL2 Antagonist/Killer (Bak)-mediated apoptosis but also promotes Notch signaling to prevent premature cell differentiation. Reducing PI3K activity destabilizes the Notch intracellular domain, while the constitutive activation of Notch reverses the PI3K deficiency phenotype. In contrast, fibroblast growth factor receptors (FGFRs) recruit Fibroblast Growth Factor Receptor Substrate 2 (Frs2) and Rous sarcoma oncogene (Src) Homology Phosphatase 2 (Shp2) to activate Mitogen-Activated Protein Kinase (MAPK) signaling, which induces the Notch ligand Jagged 1 (Jag1) and promotes cell differentiation. Inactivation of Shp2 restored the proper timing of differentiation in the p85 mutant lens, demonstrating the antagonistic interaction between FGF-induced MAPK and PDGF-induced PI3K signaling. By selective activation of PI3K and MAPK, PDGF and FGF cooperate with and oppose each other to balance progenitor cell maintenance and differentiation." @default.
- W2912649349 created "2019-02-21" @default.
- W2912649349 creator A5006651636 @default.
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- W2912649349 date "2019-02-04" @default.
- W2912649349 modified "2023-10-18" @default.
- W2912649349 title "Lens differentiation is controlled by the balance between PDGF and FGF signaling" @default.
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- W2912649349 doi "https://doi.org/10.1371/journal.pbio.3000133" @default.
- W2912649349 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6375662" @default.
- W2912649349 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30716082" @default.
- W2912649349 hasPublicationYear "2019" @default.
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