@article {Shen8903, author = {Haowei Shen and Laxminarayana Korutla and Nicholas Champtiaux and Shigenobu Toda and Ryan LaLumiere and Joseph Vallone and Matthias Klugmann and Julie A. Blendy and Scott A. Mackler and Peter W Kalivas}, title = {NAC1 Regulates the Recruitment of the Proteasome Complex into Dendritic Spines}, volume = {27}, number = {33}, pages = {8903--8913}, year = {2007}, doi = {10.1523/JNEUROSCI.1571-07.2007}, publisher = {Society for Neuroscience}, abstract = {Coordinated proteolysis of synaptic proteins is required for synaptic plasticity, but a mechanism for recruiting the ubiquitin-proteasome system (UPS) into dendritic spines is not known. NAC1 is a cocaine-regulated transcriptional protein that was found to complex with proteins in the UPS, including cullins and Mov34. NAC1 and the proteasome were cotranslocated from the nucleus into dendritic spines in cortical neurons in response to proteasome inhibition or disinhibiting synaptic activity with bicuculline. Bicuculline also produced a progressive accumulation of the proteasome and NAC1 in the postsynaptic density. Recruitment of the proteasome into dendrites and postsynaptic density by bicuculline was prevented in neurons from mice harboring an NAC1 gene deletion or in neurons transfected with mutated NAC1 lacking the proteasome binding domain. These experiments show that NAC1 modulates the translocation of the UPS from the nucleus into dendritic spines, thereby suggesting a potential missing link in the recruitment of necessary proteolysis machinery for synaptic remodeling.}, issn = {0270-6474}, URL = {https://www.jneurosci.org/content/27/33/8903}, eprint = {https://www.jneurosci.org/content/27/33/8903.full.pdf}, journal = {Journal of Neuroscience} }