New Docking Motifs in MAPKs

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Science  18 Feb 2000:
Vol. 287, Issue 5456, pp. 1169
DOI: 10.1126/science.287.5456.1169h

Binding domains are essential for the proper docking and alignment of protein partners and the subsequent transmittal of intracellular signals. Tanoue et al. have uncovered new docking motifs in the family of mitogen-activated protein kinases (MAPKs) and their upstream and downstream regulators. A small cluster of negatively charged residues, referred to as the common docking (CD) motif, interacts electrostatically with a cluster of positively charged residues found on MAPK activators, inactivators, and substrates. Coexpression studies revealed that mutation of either charged cluster abrogated protein-protein interaction, whereas in vitro experiments demonstrated that association increased kinase activity. They suggest that phosphorylation or dephosphorylation of MAPKs and the proteins that associate with them may induce conformation changes that allow one protein to dissociate as another binds to the CD motif. Such a mechanism might contribute specificity to signal transduction in MAPK pathways.—JN

Nat. Cell Biol.2, 110 (2000).

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