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The Journal of Neuroscience, August 15, 2007, 27(33):8903-8913; doi:10.1523/JNEUROSCI.1571-07.2007

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Cellular/Molecular
NAC1 Regulates the Recruitment of the Proteasome Complex into Dendritic Spines

Haowei Shen,¹ Laxminarayana Korutla,² Nicholas Champtiaux,¹ Shigenobu Toda,¹ Ryan LaLumiere,¹ Joseph Vallone,¹ Matthias Klugmann,³ Julie A. Blendy,² Scott A. Mackler,^2,4 and Peter W Kalivas¹

¹Department of Neurosciences, Medical University of South Carolina, Charleston, South Carolina 29425, ²Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, ³Department of Neurobiology, Interdisciplinary Center for Neurosciences, University of Heidelberg, Heidelberg 69123, Germany, and ⁴Departments of Medicine and Psychiatry, Philadelphia Veterans Administration Medical Center, and University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104

Correspondence should be addressed to Dr. Peter Kalivas, Department of Neurosciences, 173 Ashley Avenue, Basic Science Building 403, Medical University of South Carolina, Charleston, SC 29425. Email: kalivasp{at}musc.edu

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.

Key words: NAC1; proteasome; cullin; translocate; dendritic spine; POZ/BTB

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Received April 8, 2007; revised June 11, 2007; accepted June 28, 2007.

Correspondence should be addressed to Dr. Peter Kalivas, Department of Neurosciences, 173 Ashley Avenue, Basic Science Building 403, Medical University of South Carolina, Charleston, SC 29425. Email: kalivasp{at}musc.edu

This article has been cited by other articles:

				H.-w. Shen, S. Toda, K. Moussawi, A. Bouknight, D. S. Zahm, and P. W. Kalivas Altered Dendritic Spine Plasticity in Cocaine-Withdrawn Rats J. Neurosci., March 4, 2009; 29(9): 2876 - 2884. [Abstract] [Full Text] [PDF]

				S. Barik An intronic microRNA silences genes that are functionally antagonistic to its host gene Nucleic Acids Res., September 1, 2008; 36(16): 5232 - 5241. [Abstract] [Full Text] [PDF]

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