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Regulation of Deubiquitinating Enzymes by Post-Translational Modifications
 
 
Review

The Role of Deubiquitinating Enzymes in the Various Forms of Autophagy

Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, 1117 Budapest, Hungary
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Int. J. Mol. Sci. 2020, 21(12), 4196; https://doi.org/10.3390/ijms21124196
Received: 14 May 2020 / Revised: 9 June 2020 / Accepted: 10 June 2020 / Published: 12 June 2020
(This article belongs to the Special Issue Proteolytic Control of Deubiquitinating Enzymes in Health and Disease)
Deubiquitinating enzymes (DUBs) have an essential role in several cell biological processes via removing the various ubiquitin patterns as posttranslational modification forms from the target proteins. These enzymes also contribute to the normal cytoplasmic ubiquitin pool during the recycling of this molecule. Autophagy, a summary name of the lysosome dependent self-degradative processes, is necessary for maintaining normal cellular homeostatic equilibrium. Numerous forms of autophagy are known depending on how the cellular self-material is delivered into the lysosomal lumen. In this review we focus on the colorful role of DUBs in autophagic processes and discuss the mechanistic contribution of these molecules to normal cellular homeostasis via the possible regulation forms of autophagic mechanisms. View Full-Text
Keywords: cargo degradation; DUB; lysosome; ubiquitin; vesicle fusion cargo degradation; DUB; lysosome; ubiquitin; vesicle fusion
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MDPI and ACS Style

Csizmadia, T.; Lőw, P. The Role of Deubiquitinating Enzymes in the Various Forms of Autophagy. Int. J. Mol. Sci. 2020, 21, 4196. https://doi.org/10.3390/ijms21124196

AMA Style

Csizmadia T, Lőw P. The Role of Deubiquitinating Enzymes in the Various Forms of Autophagy. International Journal of Molecular Sciences. 2020; 21(12):4196. https://doi.org/10.3390/ijms21124196

Chicago/Turabian Style

Csizmadia, Tamás, and Péter Lőw. 2020. "The Role of Deubiquitinating Enzymes in the Various Forms of Autophagy" International Journal of Molecular Sciences 21, no. 12: 4196. https://doi.org/10.3390/ijms21124196

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