Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1862, Issue 12, Pages 2948-2954Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2018.09.009
Keywords
Ubiquitin-proteasome system; Proteasomal complexes; Ubiquitin- and ATP-independent protein degradation
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Funding
- Research Center of Redox Processes in Biomedicine (CEPID Redoxoma), Sao Paulo Research Foundation (FAPESP) [2013/07937-8]
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Background: It has been almost three decades since the removal of oxidized proteins by the free 20S catalytic unit of the proteasome (20SPT) was proposed. Since then, experimental evidence suggesting a physiological role of proteolysis mediated by the free 20SPT has being gathered. Scope of review: Experimental data that favors the hypothesis of free 20SPT as playing a role in proteolysis are critically reviewed. Major conclusions: Protein degradation by the proteasome may proceed through multiple proteasome complexes with different requirements though the unequivocal role of the free 20SPT in cellular proteolysis towards native or oxidized proteins remains to be demonstrated. General significance: The biological significance of proteolysis mediated by the free 20SPT has been elusive since its discovery. The present review critically analyzes the available experimental data supporting the proteolytic role of the free or single capped 20SPT.
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