Literature DB >> 30297324

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

Marilene Demasi1, Fernanda Marques da Cunha2.   

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.
Copyright © 2018 Elsevier B.V. All rights reserved.

Keywords:  Proteasomal complexes; Ubiquitin- and ATP-independent protein degradation; Ubiquitin-proteasome system

Mesh:

Substances:

Year:  2018        PMID: 30297324     DOI: 10.1016/j.bbagen.2018.09.009

Source DB:  PubMed          Journal:  Biochim Biophys Acta Gen Subj        ISSN: 0304-4165            Impact factor:   3.770


  6 in total

1.  Modulation of the 20S Proteasome Activity by Porphyrin Derivatives Is Steered through Their Charge Distribution.

Authors:  Marco Persico; Anna Maria Santoro; Alessandro D'Urso; Danilo Milardi; Roberto Purrello; Alessandra Cunsolo; Marina Gobbo; Roberto Fattorusso; Donatella Diana; Manuela Stefanelli; Grazia R Tundo; Diego Sbardella; Massimo Coletta; Caterina Fattorusso
Journal:  Biomolecules       Date:  2022-05-24

Review 2.  Structural Insights into Substrate Recognition and Processing by the 20S Proteasome.

Authors:  Indrajit Sahu; Michael H Glickman
Journal:  Biomolecules       Date:  2021-01-24

Review 3.  New addiction to the NRF2-related factor NRF3 in cancer cells: Ubiquitin-independent proteolysis through the 20S proteasome.

Authors:  Akira Kobayashi; Tsuyoshi Waku
Journal:  Cancer Sci       Date:  2019-12-14       Impact factor: 6.716

Review 4.  Degradation of proteins by PROTACs and other strategies.

Authors:  Yang Wang; Xueyang Jiang; Feng Feng; Wenyuan Liu; Haopeng Sun
Journal:  Acta Pharm Sin B       Date:  2019-08-13       Impact factor: 11.413

5.  Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States.

Authors:  Anna Maria Santoro; Alessandro D'Urso; Alessandra Cunsolo; Danilo Milardi; Roberto Purrello; Diego Sbardella; Grazia R Tundo; Donatella Diana; Roberto Fattorusso; Antonio Di Dato; Antonella Paladino; Marco Persico; Massimo Coletta; Caterina Fattorusso
Journal:  Int J Mol Sci       Date:  2020-09-29       Impact factor: 5.923

Review 6.  Proteasome in action: substrate degradation by the 26S proteasome.

Authors:  Indrajit Sahu; Michael H Glickman
Journal:  Biochem Soc Trans       Date:  2021-04-30       Impact factor: 5.407

  6 in total

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