Docking site peptide induced release of sequestered phosphorylation sites in the MAP kinase ERK2
نویسندگان
چکیده
منابع مشابه
Activation Mechanism of the MAP Kinase ERK2 by Dual Phosphorylation
The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase inse...
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Polarity along the anteroposterior axis of the Drosophila embryo is established by the activity of maternal gene products deposited into the egg during oogenesis. These activities direct specialised domains of zygotic gene expression required for the determination of cell fate (St. Johnston and Nüsslein-Volhard, 1992). The anterior system, which is required for the formation of the head and the...
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Mitogen-activated protein (MAP) kinases are central components of signal transduction pathways for cell proliferation, stress responses, and differentiation. Signaling efficiency and specificity are modulated in large part by docking interactions between individual MAP kinase and the kinase interaction motif (KIM), (R/K)(2-3)-X(1-6)-Phi(A)-X-Phi(B), in its cognate kinases, phosphatases, scaffol...
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The MAP kinase ERK2 is widely involved in eukaryotic signal transduction. Upon activation it translocates to the nucleus of the stimulated cell, where it phosphorylates nuclear targets. We find that nuclear accumulation of microinjected ERK2 depends on its phosphorylation state rather than on its activity or on upstream components of its signaling pathway. Phosphorylated ERK2 forms dimers with ...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2006
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.20.4.a104-c