Sequential Ubiquitination of Ribosomal Protein uS3 Triggers the Degradation of Non-functional 18S rRNA-Reference-Cited by-同舟云学术

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Sequential Ubiquitination of Ribosomal Protein uS3 Triggers the Degradation of Non-functional 18S rRNA

Published:2019-03 Issue:12 Volume:26 Page:3400-3415.e7
ISSN:2211-1247
Container-title:Cell Reports
language:en
Short-container-title:Cell Reports

Author:

Sugiyama Takato,Li Sihan,Kato Misaki,Ikeuchi Ken,Ichimura Atsushi,Matsuo Yoshitaka,Inada Toshifumi

Funder

Japan Society for the Promotion of Science

Kato Memorial Bioscience Foundation

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference51 articles.

1. Functions and regulation of the Brr2 RNA helicase during splicing;Absmeier;Cell Cycle,2016

2. Structural basis of highly conserved ribosome recycling in eukaryotes and archaea;Becker;Nature,2012

3. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control;Bengtson;Nature,2010

4. Ribosome-associated protein quality control;Brandman;Nat. Struct. Mol. Biol.,2016

5. A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress;Brandman;Cell,2012

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1. OTUD6 deubiquitination of RPS7/eS7 on the free 40 S ribosome regulates global protein translation and stress;Nature Communications;2024-08-11

2. The integrated stress response regulates 18S nonfunctional rRNA decay in mammals;2024-07-30

3. Context specific ubiquitin modification of ribosomes regulates translation under oxidative stress;2024-05-03

4. Inability to rescue stalled ribosomes results in overactivation of the integrated stress response;Journal of Biological Chemistry;2024-05

5. The kinase Rio1 and a ribosome collision-dependent decay pathway survey the integrity of 18S rRNA cleavage;PLOS Biology;2024-04-25

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