A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP

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 degrad...

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Vydáno v:	Neuron (Cambridge, Mass.) Ročník 52; číslo 2; s. 239
Hlavní autoři:	Fonseca, Rosalina, Vabulas, Ramunas M, Hartl, F Ulrich, Bonhoeffer, Tobias, Nägerl, U Valentin
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 19.10.2006
Témata:	Amino Acids - metabolism Animals Enzyme Inhibitors - pharmacology Excitatory Postsynaptic Potentials - drug effects Excitatory Postsynaptic Potentials - physiology Hippocampus - drug effects Hippocampus - metabolism Long-Term Potentiation - drug effects Long-Term Potentiation - physiology Male Nerve Tissue Proteins - biosynthesis Organ Culture Techniques Presynaptic Terminals - drug effects Presynaptic Terminals - metabolism Proteasome Endopeptidase Complex - drug effects Proteasome Endopeptidase Complex - metabolism Protein Synthesis Inhibitors - pharmacology Rats Rats, Wistar Synaptic Transmission - drug effects Synaptic Transmission - physiology Ubiquitin - metabolism
ISSN:	0896-6273
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Popis
Shrnutí:	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.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0896-6273
DOI:	10.1016/j.neuron.2006.08.015