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STEPping into Position: A New Player in the NMDA Receptor Game

Institute of Cell Biology, Department of Biology Swiss Federal Institute of Technology (ETH) Hönggerberg, CH-8093 Zürich Switzerland

SUMMARY

The posttranslational modification of proteins—phosphorylation or dephosphorylation of serine and threonine residues—is usually considered essential for the initiation and maintenance of long-term potentiation (LTP) and long-term depression (LTD) in neural plasticity. Pelkey et al. have identified at the N-methyl-D-aspartate (NMDA) receptor a protein tyrosine phosphatase—a member of the striatal-enriched phosphatase family, termed STEP₆₁—that appears to antagonize the effects of Src-mediated tyrosine phosphorylation during the facilitation of LTP. Mansuy reviews the findings of STEP₆₁ as a participant in modulating NMDA receptor-associated plasticity and discusses how differing populations of serine, threonine, and tyrosine phosphorylated or dephosphorylated residues might finely tune plasticity.