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Dynamics of integrin-mediated signaling via FAK and ERK2

机译:通过FAK和ERK2介导信号传导的动态

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Integrin-mediated signaling via focal adhesion kinase (FAK) and extracellular-signal regulated kinase 2 (ERK2) was quantified in response to modulating α5β1 integrin interaction with its fibronectin ligand. First, the dynamics of the ERK2 andFAK response were analyzed (a) to determine the dependence of each signals' kinetics on integrin-ligand bond number, (b) to gather insight into the activation and deactivation mechanisms regulating the ERK2 signal, and (c) to ascertain the disparatemechanisms that yield divergent ERK2 and FAK time-courses despite their shared integrin-ligand stimulus. Second, metrics were proposed for representing these dynamic signals with distinct time-courses. These metrics quantitatively correlated tointegrin-ligand bond number and also were related to their downstream effect on cell proliferation.
机译:响应于调节α5β1整联蛋白与其纤连蛋白配体的相互作用,量化通过焦蛋白介导的信号传导和细胞外信号调节激酶2(ERK2)。首先,分析了ERK2和FAK响应的动态(a)以确定每个信号的动力学对整合蛋白 - 配体键合数的依赖性,(b)收集调节ERK2信号的激活和失活机制的洞察力,以及(C )尽管它们共用整合素 - 配体刺激,但仍可确定产生不同的ERK2和FAK时间课程的潜在机制。其次,提出了指标,用于代表具有不同时间课程的这些动态信号。这些度量定量地相关与integrin-配体键数,也与其对细胞增殖的下游效应有关。

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