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Biomolecules 2014, 4(4), 1140-1154; doi:10.3390/biom4041140

Proteins Directly Interacting with Mammalian 20S Proteasomal Subunits and Ubiquitin-Independent Proteasomal Degradation

1
Departamento de Bioquímica, Instituto de Investigaciones Biomédicas 'Alberto Sols', UAM-CSIC, Facultad de Medicina de la Universidad Autónoma de Madrid, Madrid 28029, Spain
2
Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED) Valderrebollo 5, Madrid 28041, Spain
*
Author to whom correspondence should be addressed.
Received: 1 June 2014 / Revised: 25 November 2014 / Accepted: 11 December 2014 / Published: 19 December 2014
(This article belongs to the Special Issue Proteasomes and Its Regulators)
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Abstract

The mammalian 20S proteasome is a heterodimeric cylindrical complex (α7β7β7α7), composed of four rings each composed of seven different α or β subunits with broad proteolytic activity. We review the mammalian proteins shown to directly interact with specific 20S proteasomal subunits and those subjected to ubiquitin-independent proteasomal degradation (UIPD). The published reports of proteins that interact with specific proteasomal subunits, and others found on interactome databases and those that are degraded by a UIPD mechanism, overlap by only a few protein members. Therefore, systematic studies of the specificity of the interactions, the elucidation of the protein regions implicated in the interactions (that may or may not be followed by degradation) and competition experiments between proteins known to interact with the same proteasomal subunit, are needed. Those studies should provide a coherent picture of the molecular mechanisms governing the interactions of cellular proteins with proteasomal subunits, and their relevance to cell proteostasis and cell functioning. View Full-Text
Keywords: proteasome; proteasome interactions; ubiquitin-dependent; ubiquitin-independent; degradation; proteolysis; proteasome activators; transcription; cell cycle; neurodegeneration proteasome; proteasome interactions; ubiquitin-dependent; ubiquitin-independent; degradation; proteolysis; proteasome activators; transcription; cell cycle; neurodegeneration
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Sánchez-Lanzas, R.; Castaño, J.G. Proteins Directly Interacting with Mammalian 20S Proteasomal Subunits and Ubiquitin-Independent Proteasomal Degradation. Biomolecules 2014, 4, 1140-1154.

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