Protein synthesis-dependent formation of protein kinase Mζ in long-term potentiation

Osten, P., Valsamis, L., Harris, A., Sacktor, T. C. (1996) Protein synthesis-dependent formation of protein kinase Mζ in long-term potentiation. Journal of Neuroscience, 16 (8). pp. 2444-2451. ISSN 02706474 (ISSN)

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Abstract

The maintenance of long-term potentiation (LTP) in the CA1 region of the hippocampus has been reported to require both a persistent increase in phosphorylation and the synthesis of new proteins. The increased activity of protein kinase C (PKC) during the maintenance phase of LTP may result from the formation of PKMζ, the constitutively active fragment of a specific PKC isozyme. To define the relationship among PKMζ, longterm EPSP responses, and the requirement for new protein synthesis, we examined the regulation of PKMζ after subthreshold stimulation that produced short-term potentiation (STP) and after suprathreshold stimulation by single and multiple tetanic trains that produced LTP. We found that, although no persistent increase in PKMζ followed STP, the degree of long-term EPSP potentiation was linearly correlated with the increase of PKMζ. The increase was first observed 10 min after a tetanus that induced LTP and lasted for at least 2 hr, in parallel with the persistence of EPSP enhancement. Both the maintenance of LTP and the long-term increase in PKMζ were blocked by the protein synthesis inhibitors anisomycin and cycloheximide. These results suggest that PKMζ is a component of a protein synthesis-dependent mechanism for persistent phosphorylation in LTP.

Item Type: Paper
Uncontrolled Keywords: learning and memory long-term potentiation LTP maintenance phosphorylation PKMζ protein kinase C zeta isozyme anisomycin cycloheximide protein kinase animal tissue article brain slice controlled study excitatory postsynaptic potential hippocampus immunoblotting learning long term potentiation memory nonhuman priority journal protein phosphorylation protein synthesis rat Animals Immunohistochemistry Membrane Potentials Protein Kinases Time Factors
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > Long term potentiation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Osten lab
Depositing User: Matt Covey
Date: 1996
Date Deposited: 04 Apr 2013 21:11
Last Modified: 04 Apr 2013 21:11
Related URLs:
URI: https://repository.cshl.edu/id/eprint/28093

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