A Balance of Protein Synthesis and Proteasome-Dependent Degradation Determines the Maintenance of LTP
Neuron. 2006-10-01; 52(2): 239-245
DOI: 10.1016/j.neuron.2006.08.015
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1. Neuron. 2006 Oct 19;52(2):239-45.
A balance of protein synthesis and proteasome-dependent degradation determines
the maintenance of LTP.
Fonseca R(1), Vabulas RM, Hartl FU, Bonhoeffer T, Nägerl UV.
Author information:
(1)Department of Cellular and Systems Neurobiology, Max Planck Institute of
Neurobiology, Am Klopferspitz 18, 82152 München-Martinsried, Germany.
Long-lasting changes in synaptic strength are thought to play a pivotal role in
activity-dependent plasticity and memory. There is ample evidence indicating that
in hippocampal long-term potentiation (LTP) the synthesis of new proteins is
crucial for enduring changes. However, whether protein degradation also plays a
role in this process has only recently begun to receive attention. Here, we
examine the effects of blocking protein degradation on LTP. We show that
pharmacological inhibition of proteasome-dependent protein degradation, just like
inhibition of protein synthesis, disrupts expression of late (L-)LTP. However,
when protein degradation and protein synthesis are inhibited at the same time,
LTP is restored to control levels, calling into question the commonly held
hypothesis that synthesis of new proteins is indispensable for L-LTP. Instead,
these findings point to a more facetted model, in which L-LTP is determined by
the combined action of synthesis and degradation of plasticity proteins.
DOI: 10.1016/j.neuron.2006.08.015
PMID: 17046687 [Indexed for MEDLINE]