4.4 Review

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases

Journal

BMB REPORTS
Volume 49, Issue 9, Pages 459-473

Publisher

KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2016.49.9.094

Keywords

Assembly; Gate opening; Neurodegenerative diseases; Post-translational modification; Proteasome; Regulators

Funding

  1. National Research Foundation of Korea (NRF) - Ministry of Science, ICT & Future Planning (MSIP), Republic of Korea [2015R1A2A2A01003 080, 2014M3C7A1064545]
  2. Korea Healthcare Technology R&D Project through the Korea Health Industry Development Institute (KHIDI) - Ministry of Health & Welfare, Republic of Korea [HI14C0093]
  3. Yonsei University Research Fund [2014-12-0134]
  4. Yonsei University Future-leading Research Initiative [2015-22-0055]

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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 NDs 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.

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