Blm10 Protein Promotes Proteasomal Substrate Turnover by an Active Gating Mechanism

被引：68

作者：

Dange, Thomas ^{[1
]}

Smith, David ^{[2
]}

Noy, Tahel ^{[1
]}

Rommel, Philipp C. ^{[1
]}

Jurzitza, Lukas ^{[1
]}

Cordero, Radames J. B. ^{[1
]}

Legendre, Anne ^{[2
]}

Finley, Daniel ^{[2
]}

Goldberg, Alfred L. ^{[2
]}

Schmidt, Marion ^{[1
]}

机构：

[1] Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA

[2] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2011年 / 286卷 / 50期

基金：

美国国家卫生研究院;

关键词：

20; S-PROTEASOMES; SACCHAROMYCES-CEREVISIAE; PROTEOLYTIC MACHINE; REGULATORY PARTICLE; GENE DISRUPTION; 26S PROTEASOME; CORE PARTICLE; C-TERMINI; ATPASES; COMPLEX;

D O I：

10.1074/jbc.M111.300178

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Background: Association of the proteasome core with activators regulates proteasome activity. Results: Blm10 association increases proteasome activity toward peptides and the unstructured proteasome substrate tau-441. This process is mediated by the C terminus of Blm10. Conclusion: C-terminal docking-mediated proteasome activation by Blm10 facilitates the turnover of peptide and protein substrates. Significance: Blm10 contributes to the regulation of proteasome activity.

引用

页码：42830 / 42839

页数：10

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