Exploiting the difference between intrinsic and extrinsic kinases: implications for regulation of signaling by immunoreceptors.

作者: U M Kent , C Torigoe , B Goldstein , C Wofsy , H Metzger

DOI:

关键词: Receptor tyrosine kinaseMAPK14MAPK7ASK1Proto-oncogene tyrosine-protein kinase SrcLYNG protein-coupled receptor kinaseBiologyTyrosine phosphorylationCell biology

摘要: When receptors must interact with an extrinsic kinase to initiate signaling, the can play a regulatory role that is not available intrinsic receptor kinases. Whether control exercised at this level depends critically on amount of and potential for redistribution during signaling. This study demonstrates high affinity IgE (Fc epsilonRI) rat basophilic leukemia cells regulated by its initiating kinase. We present mathematical model allows reversible recruitment kinases phosphorylated immunoreceptor tyrosine-based activation motifs. By comparing predictions experimental time courses phosphorylation, we infer Lyn limiting, occurs after are aggregated, makes relationship between tyrosine phosphorylation aggregation nonlinear.

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