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文献和实验Cell-Free Assay System for Ras- and Rap1-Dependent Activation of MAP-Kinase Cascade
4 ). MAP kinase is phosphorylated at both serme/threonme and tyrosine residues by MEK and this phosphorylation causes the MAP-kinase activation (1 –3 ). MEK is also phosphorylated at serine/threonme residues by MEK kinase, and this phosphorylation causes
Fluorescence Microscopy Study of Rap1 Subcellular Localization
The Ras-related GTPase Rap has been implicated in multiple cellular functions. In particular, Rap1 is a crucial regulator of both inside-out integrin activation and outside-in E-cadherin-mediated signaling. Thus, Rap1
Pull-Down Assay for Analysis of Integrin-Mediated Activation of Rap Proteins in Adherent Platelets
high levels of Rap1 proteins, mainly Rap1b, which plays a critical role in platelet adhesion and activation. Rap1 is a key element in the inside-out signaling pathway leading to the conversion of integrins into the high-affinity
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