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kin(p(HGNC:EGFR)) -> p(HGNC:PAG1,pmod(P,Y,317))
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Approximately 61,000 statements.
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Recently, we and others (8, 9) have identified a transmembrane phosphoprotein, known as Csk-binding protein (Cbp) or phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), which binds tightly to the SH2 domain of Csk. Cbp is located exclusively in so-called lipid rafts in which cholesterol, glycosphingolipid, and a variety of membrane-anchored signaling molecules including SFK accumulate. Lipid rafts are thus viewed as platforms for signaling across the membrane. The interaction of Cbp with Csk is also dependent upon the phosphorylation of its Tyr-314 by SFK (8-10). Based on these lines of evidence, a model of feedback regulation of SFK has been presented according to which activation of SFK by an extracellular stimulus leads to the phosphorylation of Cbp; this results in recruitment of Csk to lipid rafts and is followed by termination of SFK function (11-13).
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2014-07-03T14:32:12.013+02:00
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