Blm10 Protein Promotes Proteasomal Substrate Turnover by an Active Gating Mechanism

被引：70

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

共 54 条

[41] Proteasome-associated proteins: regulation of a proteolytic machine [J].

Schmidt, M ;

Hanna, J ;

Elsasser, S ;

Finley, D .

BIOLOGICAL CHEMISTRY, 2005, 386 (08) :725-737

[42] The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle [J].

Schmidt, M ;

Haas, W ;

Crosas, B ;

Santamaria, PG ;

Gygi, SP ;

Walz, T ;

Finley, D .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2005, 12 (04) :294-303

[43] Targeting Proteins for Destruction by the Ubiquitin System: Implications for Human Pathobiology [J].

Schwartz, Alan L. ;

Ciechanover, Aaron .

ANNUAL REVIEW OF PHARMACOLOGY AND TOXICOLOGY, 2009, 49 :73-96

[44] Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's α ring opens the gate for substrate entry [J].

Smith, David M. ;

Chang, Shih-Chung ;

Park, Soyeon ;

Finley, Daniel ;

Cheng, Yifan ;

Goldberg, Alfred L. .

MOLECULAR CELL, 2007, 27 (05) :731-744

[45] ATP Binds to Proteasomal ATPases in Pairs with Distinct Functional Effects, Implying an Ordered Reaction Cycle [J].

Smith, David M. ;

Fraga, Hugo ;

Reis, Christian ;

Kafri, Galit ;

Goldberg, Alfred L. .

CELL, 2011, 144 (04) :526-538

[46] ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins [J].

Smith, DM ;

Kafri, G ;

Cheng, YF ;

Ng, D ;

Walz, T ;

Goldberg, AL .

MOLECULAR CELL, 2005, 20 (05) :687-698

[47] Proteasome Activators [J].

Stadtmueller, Beth M. ;

Hill, Christopher P. .

MOLECULAR CELL, 2011, 41 (01) :8-19

[48] Heterohexameric Ring Arrangement of the Eukaryotic Proteasomal ATPases: Implications for Proteasome Structure and Assembly [J].

Tomko, Robert J., Jr. ;

Funakoshi, Minoru ;

Schneider, Kyle ;

Wang, Jimin ;

Hochstrasser, Mark .

MOLECULAR CELL, 2010, 38 (03) :393-403

[49] PA200, a nuclear proteasome activator involved in DNA repair [J].

Ustrell, V ;

Hoffman, L ;

Pratt, G ;

Rechsteiner, M .

EMBO JOURNAL, 2002, 21 (13) :3516-3525

[50] Structural basis for the activation of 20S proteasomes by 11S regulators [J].

Whitby, FG ;

Masters, EI ;

Kramer, L ;

Knowlton, JR ;

Yao, Y ;

Wang, CC ;

Hill, CP .

NATURE, 2000, 408 (6808) :115-120

← 1 2 3 4 5 6 →