sg:pub.10.1134/s000629790913001x - Springer Nature SciGraph

Article Info

DATE

2009-12

AUTHORS

A. V. Sorokin, E. R. Kim, L. P. Ovchinnikov

ABSTRACT

In eukaryotic cells, degradation of most intracellular proteins is realized by proteasomes. The substrates for proteolysis are selected by the fact that the gate to the proteolytic chamber of the proteasome is usually closed, and only proteins carrying a special "label" can get into it. A polyubiquitin chain plays the role of the "label": degradation affects proteins conjugated with a ubiquitin (Ub) chain that consists at minimum of four molecules. Upon entering the proteasome channel, the polypeptide chain of the protein unfolds and stretches along it, being hydrolyzed to short peptides. Ubiquitin per se does not get into the proteasome, but, after destruction of the "labeled" molecule, it is released and labels another molecule. This process has been named "Ub-dependent protein degradation". In this review we systematize current data on the Ub-proteasome system, describe in detail proteasome structure, the ubiquitination system, and the classical ATP/Ub-dependent mechanism of protein degradation, as well as try to focus readers' attention on the existence of alternative mechanisms of proteasomal degradation and processing of proteins. Data on damages of the proteasome system that lead to the development of different diseases are given separately. More... »

PAGES

1411-1442

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Journal

TITLE

Biochemistry (Moscow)

ISSUE

VOLUME

Subjects

FOR: Biochemistry And Cell Biology

FOR: Biological Sciences

MESH: Adenosine Triphosphate

MESH: Animals

MESH: Disease

MESH: Eukaryotic Cells

MESH: Humans

MESH: Neoplasms

MESH: Proteasome Endopeptidase Complex

MESH: Protein Subunits

MESH: Proteins

MESH: Ubiquitin

Author Affiliations

Institute of Protein Research

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s000629790913001x

DOI

http://dx.doi.org/10.1134/s000629790913001x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040426961

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20210701

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