Abstract
Ubiquitin can be detected in the neuronal and glial inclusions that are the diagnostic hallmarks of a number of human neurodegenerative diseases. It has been assumed that the presence of ubiquitin signifies the failed attempt of the cell to remove abnormal protein structures, which have been allowed to aggregate. The burden of abnormal protein arising from genetic mutations or cumulative oxidative damage might in the course of time overwhelm the ubiquitin-proteasome pathway (whose responsibility it is to eliminate misfolded or damaged proteins). However, ubiquitin may still serve a protective purpose distinct from its role in proteolysis. The physical properties of ubiquitin are such that a surface coating of ubiquitin should preclude further growth of the aggregate, prevent non-productive interactions, and conceal the contents from detection mechanisms that might ultimately kill the cell. This 'nonstick coating' hypothesis makes predictions about the nature of the conjugated ubiquitin and the consequences of removing it.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.