Significance of 14-3-3 Self-Dimerization for Phosphorylation-dependent Target Binding

Eitemau Tebyg

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• Identification of Raf-1 S471 as a Novel Phosphorylation Site Critical for Raf-1 and B-Raf Kinase Activities and for MEK Binding
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• Activation of the plant plasma membrane H(+)-ATPase by phosphorylation and binding of 14-3-3 proteins converts a dimer into a hexamer
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• Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association.
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• Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding
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