BMB Rep. 2016; 49(9): 459-473  
Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases
Eunju Im#,* & Kwang Chul Chung*
Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea
Correspondence to: Kwang Chul Chung, Tel: +82-2-2123-2653; Fax: +82-2-312-5657; E-mail: kchung@yonsei.ac.kr, Eunju Im, Tel: +1-845-398-5438; Fax: +1-845-398-2179; E-mail: eim@nki.rfmh.org
#Present Affiliation: Center for Dementia Research, Nathan S. Kline Institute for Psychiatric Research, Orangeburg, NY 10962, USA. Department of Psychiatry, New York University School of Medicine, New York, NY 10016, USA
Received: June 9, 2016; Published online: September 30, 2016.
© Korean Society for Biochemistry and Molecular Biology. All rights reserved.

Abstract
Neurodegenerative diseases (NDs) often involve the formation of abnormal and toxic protein aggregates, which are thought to be the primary factor in ND occurrence and progression. Aged neurons exhibit marked increases in aggregated protein levels, which can lead to increased cell death in specific brain regions. As no specific drugs/therapies for treating the symptoms or/and progression of DDs are available, obtaining a complete understanding of the mechanism underlying the formation of protein aggregates is needed for designing a novel and efficient removal strategy. Intracellular proteolysis generally involves either the lysosomal or ubiquitin-proteasome system. In this review, we focus on the structure and assembly of the proteasome, proteasome-mediated protein degradation, and the multiple dynamic regulatory mechanisms governing proteasome activity. We also discuss the plausibility of the correlation between changes in proteasome activity and the occurrence of NDs.
Keywords: Assembly, Gate opening, Neurodegenerative diseases, Post-translational modification, Proteasome, Regulators


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