A novel crosstalk between two major protein degradation systems Regulation of proteasomal activity by autophagy
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AbstractEukaryotes have two major intracellular protein degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Inhibition of proteasomal activities has been previously shown to induce autophagy, indicating a coordinated and complementary relationship between these two systems. However, little is known about the regulation of the UPS by autophagy. In this study, we showed for the first time that proteasomes were activated in response to pharmacological inhibition of autophagy as well as disruption of autophagy-related genes by RNA interference under nutrient-deficient conditions in cultured human colon cancer cells. The induction was evidenced by the increased proteasomal activities and the upregulation of proteasomal subunits, including the proteasome 5 subunit, PSMB5. Co-inhibition of the proteasome and autophagy also synergistically increased the accumulation of polyubiquitinated proteins. Collectively, our findings suggest that proteasomes are activated in a compensatory manner for protein degradation upon autophagy inhibition. Our studies unveiled a novel regulatory mechanism between the two protein degradation pathways.
All Author(s) ListWang XJ, Yu J, Wong SH, Cheng ASL, Chan FKL, Ng SSM, Cho CH, Sung JJY, Wu WKK
Journal nameAutophagy
Volume Number9
Issue Number10
PublisherTaylor & Francis: STM, Behavioural Science and Public Health Titles
Pages1500 - 1508
LanguagesEnglish-United Kingdom
Keywordsautophagy; chloroquine; proteasome; protein degradation; SQSTM1
Web of Science Subject CategoriesCell Biology; CELL BIOLOGY

Last updated on 2020-28-05 at 01:30