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

被引：22

作者：

Demasi, Marilene ^{[1
]}

da Cunha, Fernanda Marques ^{[2
]}

机构：

[1] Inst Butantan, Lab Bioquim & Biofis, Sao Paulo, SP, Brazil

[2] Univ Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Sao Paulo, SP, Brazil

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2018年 / 1862卷 / 12期

基金：

巴西圣保罗研究基金会;

关键词：

Ubiquitin-proteasome system; Proteasomal complexes; Ubiquitin- and ATP-independent protein degradation; 26S PROTEASOME; OXIDIZED PROTEINS; OXYGEN RADICALS; DEPENDENT DEGRADATION; DISTINCT ROLES; UBIQUITIN; ATP; COMPLEX; CELLS; MECHANISMS;

D O I：

10.1016/j.bbagen.2018.09.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2948 / 2954

页数：7

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