Literature DB >> 22350895

Assembly and function of the proteasome.

Yasushi Saeki1, Keiji Tanaka.   

Abstract

Proteasome is a highly organized protease complex comprising a catalytic 20S core particle (CP) and two 19S regulatory particles (RP), which together form the 26S structure. The 26S proteasome is responsible for the degradation of most ubiquitylated proteins through a multistep process involving recognition of the polyubiquitin chain, unfolding of the substrate, and translocation of the substrate into the active site in the cavity of the CP. Recent studies have shed light on various aspects of the complex functions of the 26S proteasome. In addition, the recent identification of various proteasome-dedicated chaperones indicates that the assembly pathways of the RP and CP are multistep processes. In this review, we summarize recent advances in the understanding of the proteasome structure, function, and assembly.

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Year:  2012        PMID: 22350895     DOI: 10.1007/978-1-61779-474-2_22

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  45 in total

1.  High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx.

Authors:  Zhanyu Ding; Zhenglin Fu; Cong Xu; Yifan Wang; Yanxing Wang; Junrui Li; Liangliang Kong; Jinhuan Chen; Na Li; Rongguang Zhang; Yao Cong
Journal:  Cell Res       Date:  2017-01-20       Impact factor: 25.617

2.  Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation.

Authors:  Simone Stork; Daniel Moog; Jude M Przyborski; Ilka Wilhelmi; Stefan Zauner; Uwe G Maier
Journal:  Eukaryot Cell       Date:  2012-10-05

3.  Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation.

Authors:  Evan J Worden; Chris Padovani; Andreas Martin
Journal:  Nat Struct Mol Biol       Date:  2014-01-23       Impact factor: 15.369

4.  The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.

Authors:  G R Tundo; D Sbardella; A M Santoro; A Coletta; F Oddone; G Grasso; D Milardi; P M Lacal; S Marini; R Purrello; G Graziani; M Coletta
Journal:  Pharmacol Ther       Date:  2020-05-19       Impact factor: 12.310

5.  Ablation of Immunoproteasome β5i Subunit Suppresses Hypertensive Retinopathy by Blocking ATRAP Degradation in Mice.

Authors:  Shuai Wang; Jing Li; Tong Wang; Jie Bai; Yun-Long Zhang; Qiu-Yue Lin; Jing-Min Li; Qi Zhao; Shu-Bin Guo; Hui-Hua Li
Journal:  Mol Ther       Date:  2019-10-05       Impact factor: 11.454

Review 6.  Proteasome Structure and Assembly.

Authors:  Lauren Budenholzer; Chin Leng Cheng; Yanjie Li; Mark Hochstrasser
Journal:  J Mol Biol       Date:  2017-06-03       Impact factor: 5.469

7.  Overexpression of USP14 protease reduces I-κB protein levels and increases cytokine release in lung epithelial cells.

Authors:  Rachel K Mialki; Jing Zhao; Jianxin Wei; Daniel F Mallampalli; Yutong Zhao
Journal:  J Biol Chem       Date:  2013-04-24       Impact factor: 5.157

8.  Structural insights into proteasome activation by the 19S regulatory particle.

Authors:  Aaron Ehlinger; Kylie J Walters
Journal:  Biochemistry       Date:  2013-05-14       Impact factor: 3.162

Review 9.  Gates, Channels, and Switches: Elements of the Proteasome Machine.

Authors:  Daniel Finley; Xiang Chen; Kylie J Walters
Journal:  Trends Biochem Sci       Date:  2015-11-28       Impact factor: 13.807

10.  New insight into the mechanism underlying the silk gland biological process by knocking out fibroin heavy chain in the silkworm.

Authors:  Yong Cui; Yanan Zhu; Yongjian Lin; Lei Chen; Qili Feng; Wen Wang; Hui Xiang
Journal:  BMC Genomics       Date:  2018-03-26       Impact factor: 3.969

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