Regulatory Role of Ubiquitin Specific Protease-13 (USP13) in Misfolded Protein Clearance in Neurodegenerative Diseases.

Neuroscience

Translational Neurotherapeutics Program, Laboratory for Dementia and Parkinsonism, Department of Neurology, Georgetown University Medical Center, Building D, Room 265, 4000 Reservoir Road, NW, Washington DC 20057, USA. Electronic address:

Published: April 2021

AI Article Synopsis

  • USP-13 is a de-ubiquitinase that removes ubiquitin from proteins, reversing their degradation and is linked to neurodegenerative diseases.
  • Ubiquitin marks proteins for degradation by cellular pathways like the proteasome and lysosome, with USP13 playing a role in this process, especially in melanoma cells.
  • The review highlights the current understanding of USP13's involvement in regulating protein clearance through autophagy and the proteasome in the context of neurodegeneration.

Article Abstract

Ubiquitin Specific Protease (USP)-13 is a de-ubiquitinase member of the cysteine-dependent protease superfamily that cleaves ubiquitin off protein substrates to reverse ubiquitin-mediated protein degradation. Several findings implicate USPs in neurodegeneration. Ubiquitin targets proteins to major degradation pathways, including the proteasome and the lysosome. In melanoma cells, USP13 regulates the degradation of several proteins primarily via ubiquitination and de-ubiquitination. However, the significance of USP13 in regulating protein clearance in neurodegeneration is largely unknown. This mini-review summarizes the most recent evidence pertaining to the role of USP13 in protein clearance via autophagy and the proteasome in neurodegenerative diseases.

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Source
http://dx.doi.org/10.1016/j.neuroscience.2021.02.004DOI Listing

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