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Sci. Signal., 9 March 2010
Vol. 3, Issue 112, p. ra18
[DOI: 10.1126/scisignal.2000451]

RESEARCH ARTICLES

Editor's Summary

Pinning Down LTP
The late phase of long-term potentiation (L-LTP), a persistent use-dependent increase in the efficacy of glutamatergic synapses believed to underlie some forms of memory, depends on new protein synthesis in dendrites. Noting that peptidyl-prolyl isomerases (PPIases) have been implicated in L-LTP, Westmark et al. investigated the role of the PPIase Pin1 in dendritic protein synthesis and LTP. They found that catalytically active Pin1 was present in dendrites, where it associated with eukaryotic translation initiation factor 4E (eIF4E) and the eIF4E-binding proteins 4E-BP1 and 2 and inhibited translation. Glutamate inhibited Pin1 activity and relieved its suppression of translation. Maintenance of L-LTP depends on the activity of protein kinase M {zeta} (PKM{zeta}, a constitutively active isoform of PKC), and mice lacking Pin1 showed both increased PKM{zeta} abundance and enhanced L-LTP. PKM{zeta} inhibited Pin1 activity and promoted translation. The authors thus propose that LTP depends on interactions among Pin1, PKM{zeta}, and translation: Pin1-dependent inhibition of PKM{zeta} translation is relieved by glutamatergic signaling, allowing PKM{zeta}, in turn, to inhibit Pin1, thereby maintaining dendritic translation and L-LTP.

Citation: P. R. Westmark, C. J. Westmark, S. Wang, J. Levenson, K. J. O’Riordan, C. Burger, J. S. Malter, Pin1 and PKM{zeta} Sequentially Control Dendritic Protein Synthesis. Sci. Signal. 3, ra18 (2010).

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