Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis

Article Abstract:

A point mutation causes the fibroblast growth factor (FGF) receptor to lose its ability to link with the tyrosine-phosphorylate phospholipase C-gamma (PLC-gamma) or to bring about the hydrolysis of phosphatidylinositol. This point mutation involves the insertion of a phenylalanine residue (Y766F) in place of Tyr 766. However, the Y766F FGF receptor mutant is capable of autophosphorylation. Loss of phosphatidylinositol hydrolysis does not impair FGF-stimulated mitogenesis despite the importance of Tyr 766 phosphorylation for PLC-gamma phosphorylation and for phosphatidylinositol hydrolysis.

Phosphorylation

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Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis

Article Abstract:

Fibroblast growth factor (FGF) receptor with a point mutation will no longer link with phospholipase C-gamma (PLC-gamma). This point mutation involves phenylalanine taking the place of tyrosine at residue 766. In addition, the mutant receptor will no longer regulate the hydrolysis of phosphatidylinositol (PtdIns) of the formation of Ca2+ following FGF stimulation. Hence the point mutation of the FGF receptor can sometimes stop activation of PLC-gamma. Moreover, FGF-induced mitogenesis can happen without Ca2+ mobilization or PtdIns hydrolysis.

Calcium ions, Phospholipases

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Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling

Article Abstract:

SH3 domains of Grb2 couple with hSos1's carboxy-terminal. This terminal is a human homologue of Drosophila guanine-nucleotide-releasing factor for Ras, which affects the command of Ras activity by epidermal growth factor (EGF) receptors. SH3 and hSos1 interaction illustrates a leap in conserved signalling pathway for regulation of cell growth and differentiation. Grb2/hSos1 complex couples induce EGF recepto to Ras signalling. But this interaction can be suppressed by a synthetic 10-amino-acid peptide having PPVPPR sequence.

Analysis, Cell interaction, Cell interactions, G proteins, Epidermal growth factor, Epidermal growth factors

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