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Dendritic Transport and Localization of Protein Kinase M zeta mRNA: IMPLICATIONS FOR MOLECULAR MEMORY CONSOLIDATION

Protein kinase M zeta (PKM zeta ) is an atypical protein kinase C isoform that has been implicated in the protein synthesis-dependent maintenance of long term potentiation and memory storage in the brain. Synapse-associated kinases are uniquely positioned to promote enduring consolidation of structu...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-12, Vol.279 (50), p.52613-52622
Main Authors: Muslimov, Ilham Aliagaevich, Nimmrich, Volker, Hernandez, Alejandro Ivan, Tcherepanov, Andrew, Sacktor, Todd Charlton, Tiedge, Henri
Format: Article
Language:English
Online Access:Get full text
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Summary:Protein kinase M zeta (PKM zeta ) is an atypical protein kinase C isoform that has been implicated in the protein synthesis-dependent maintenance of long term potentiation and memory storage in the brain. Synapse-associated kinases are uniquely positioned to promote enduring consolidation of structural and functional modifications at the synapse, provided that kinase mRNA is available on site for local input-specific translation. We now report that the mRNA encoding PKM zeta is rapidly transported and specifically localized to synaptodendritic neuronal domains. Transport of PKM zeta mRNA is specified by two cis-acting dendritic targeting elements (M zeta DTEs). M zeta DTE1, located at the interface of the 5'-untranslated region and the open reading frame, directs somato-dendritic export of the mRNA. M zeta DTE2, in contrast, is located in the 3'-untranslated region and is required for delivery of the mRNA to distal dendritic segments. Colocalization with translational repressor BC1 RNA in hippocampal dendrites suggests that PKM zeta mRNA may be subject to translational control in local domains. Dendritic localization of PKM zeta mRNA provides a molecular basis for the functional integration of synaptic signal transduction and translational control pathways.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M409240200