EGFR interacts with phospholipase C-gamma
نویسندگان
چکیده
منابع مشابه
Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes.
The lipase activity of most phospholipases C (PLCs) is basally repressed by a highly degenerate and mostly disordered X/Y linker inserted within the catalytic domain. Release of this auto-inhibition is driven by electrostatic repulsion between the plasma membrane and the electronegative X/Y linker. In contrast, PLC-γ isozymes (PLC-γ1 and -γ2) are structurally distinct from other PLCs because mu...
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Binding of ligand to the alpha subunit of Fc gamma RIIIA(CD16), expressed at the natural killer (NK) cell membrane in association with homo or heterodimers of proteins of the zeta family, results in phosphorylation of several proteins on tyrosine residues. We have analyzed the role of protein tyrosine phosphorylation in the regulation of molecular events induced upon stimulation of Fc gamma RII...
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Association of phospholipase C (PLC)-gamma 1 with the cytoskeleton has been postulated to be one of the crucial steps for PLC-gamma 1 activation and translocation to the plasma membrane. In this report, direct binding assays were carried out to study which fragment of PLC-gamma 1 Src homology region has been able to bind to the actin-cytoskeleton. Using GST fusion proteins containing various de...
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ژورنال
عنوان ژورنال: Reactome - a curated knowledgebase of biological pathways
سال: 2008
ISSN: 1934-1792
DOI: 10.3180/react_12478.1