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• W2100646739 endingPage "7406" @default.
• W2100646739 startingPage "7398" @default.
• W2100646739 abstract "Substitution of phenylalanine for tyrosine at codon 809 (Y809F) of the human colony-stimulating factor 1 (CSF-1) receptor (CSF-1R) impairs ligand-stimulated tyrosine kinase activity, prevents induction of c-MYC and cyclin D1 genes, and blocks CSF-1-dependent progression through the G1 phase of the cell cycle. We devised an unbiased genetic screen to isolate genes that restore the ability of CSF-1 to stimulate growth in cells that express mutant CSF-1R (Y809F). This screen led us to identify a truncated form of the murine type Ibeta phosphatidylinositol 4-phosphate 5-kinase (mPIP5K-Ibeta). This truncated protein lacks residues 1 to 238 of mPIP5K-Ibeta and is catalytically inactive. When we transfected cells expressing CSF-1R (Y809F) with mPIP5K-Ibeta (delta1-238), CSF-1-dependent induction of c-MYC and cyclin D1 was restored and ligand-dependent cell proliferation was sustained. CSF-1 normally triggers the rapid disappearance of CSF-1R (Y809F) from the cell surface; however, transfection of cells with mPIP5K-Ibeta (delta1-238) stabilized CSF-1R (Y809F) expression on the cell surface, resulting in elevated levels of ligand-activated CSF-1R (Y809F). These results suggest a role for PIP5K-Ibeta in receptor endocytosis and that the truncated enzyme compensated for a mitogenically defective CSF-1R by interfering with this process." @default.
• W2100646739 created "2016-06-24" @default.
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• W2100646739 date "1997-12-01" @default.
• W2100646739 modified "2023-10-11" @default.
• W2100646739 title "Complementation of Growth Factor Receptor-Dependent Mitogenic Signaling by a Truncated Type I Phosphatidylinositol 4-Phosphate 5-Kinase" @default.
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• W2100646739 doi "https://doi.org/10.1128/mcb.17.12.7398" @default.
• W2100646739 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/232595" @default.
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