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Updated: Oct 22, 2025

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
Published on: May 21, 2019
20S and 26S proteasome-binding proteins of the rabbit brain: A proteomic dataset
Olga Buneeva1, Arthur Kopylov1, Svetlana Kaloshina1
1Institute of Biomedical Chemistry, 10 Pogodinskaya street, Moscow 119121 Russian Federation.
Abstract:
Fractions of 26S and 20S proteasomes isolated from the rabbit brain by the method of salt fractionation (salt-induced precipitation) contain intrinsic proteasome proteins responsible for assembly of the core particle and regulatory particle of proteasome and also proteasome-binding proteins. These proteasome-binding proteins include components of the ubiquitin-proteasome system, some ubiquitinated proteins, as well as cytoskeleton components, protective proteins, regulators of gene expression, cell division, and differentiation, and multifunctional proteins (mainly, glycolytic enzymes: glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aldolase, pyruvate kinase, etc.). The multifunctional proteins also known as "moonlighting proteins" are involved in various (regulatory) processes in the cell and obviously represent important components of the proteasome interactome rather than contaminants of the 26S and 20S proteasome fractions.
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