Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 25, Pages 17758-17766Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.544247
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Funding
- Russian Scientific Foundation [14-14-00585]
- Russian Foundation for Basic Research [12-04-33258, 12-04-01609-a]
- Russian Federation [CPi 2445.2013.4]
- Skolkovo program
- RFBR [10-04-00673, 13-04-40277-H]
- Scientific School Support Program Chemical Basis of Biocatalysis [2046.2012.4]
- Presidium of the Russian Academy of Sciences [24]
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- Israel Science Foundation
- I-CORE Program of the Planning and Budgeting Committee
- Israel Science Foundation [1775/12]
- European Union Treat PolyQ Network
- Deutsch-Israelische Projektkooperation
- Russian Science Foundation [14-14-00585] Funding Source: Russian Science Foundation
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The vast majority of cellular proteins are degraded by the 26S proteasome after their ubiquitination. Here, we report that the major component of the myelin multilayered membrane sheath, myelin basic protein (MBP), is hydrolyzed by the 26S proteasome in a ubiquitin-independent manner both in vitro and in mammalian cells. As a proteasomal substrate, MBP reveals a distinct and physiologically relevant concentration range for ubiquitin-independent proteolysis. Enzymatic deimination prevents hydrolysis of MBP by the proteasome, suggesting that an abnormally basic charge contributes to its susceptibility toward proteasome-mediated degradation. To our knowledge, our data reveal the first case of a pathophysiologically important autoantigen as a ubiquitin-independent substrate of the 26S proteasome.
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