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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The physiological role of the free 20S proteasome in protein degradation: A critical review

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Author(s):
Demasi, Marilene [1] ; da Cunha, Fernanda Marques [2]
Total Authors: 2
Affiliation:
[1] Inst Butantan, Lab Bioquim & Biofis, Sao Paulo, SP - Brazil
[2] Univ Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Sao Paulo, SP - Brazil
Total Affiliations: 2
Document type: Review article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS; v. 1862, n. 12, p. 2948-2954, DEC 2018.
Web of Science Citations: 5
Abstract

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. (AU)

FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC