研究者業績

井澤 俊明

イザワ トシアキ  (Izawa Toshiaki)

基本情報

所属
兵庫県立大学 大学院理学研究科 准教授
学位
博士(理学)(2012年5月 名古屋大学)

研究者番号
60837871
J-GLOBAL ID
201801005029524793
researchmap会員ID
B000329969

論文

 17
  • Ting Su, Toshiaki Izawa, Matthias Thoms, Yui Yamashita, Jingdong Cheng, Otto Berninghausen, F. Ulrich Hartl, Toshifumi Inada, Walter Neupert, Roland Beckmann
    Nature 571(7764) E4 2019年7月11日  
    In Fig. 2g of this Letter, owing to an error during the production process, the bottom blot for ‘IB: Myc’ was missing. The original Letter has been corrected online.
  • Su T, Izawa T (Co-first author), Thoms M, Yamashita Y, Cheng J, Berninghausen O, Hartl FU, Inada T, Neupert W, Beckmann R
    Nature 570(7762) 538-542 2019年6月  査読有り
  • Hashimoto S, Nobuta R, Izawa T, Inada T
    FEBS letters 593(8) 777-787 2019年4月  査読有り
  • Ken Ikeuchi, Toshiaki Izawa, Toshifumi Inada
    Frontiers in genetics 9 743-743 2018年  査読有り
    Accurate gene expression is a prerequisite for all cellular processes. Cells actively promote correct protein folding, which prevents the accumulation of abnormal and non-functional proteins. Translation elongation is the fundamental step in gene expression to ensure cellular functions, and abnormal translation arrest is recognized and removed by the quality controls. Recent studies demonstrated that ribosome plays crucial roles as a hub for gene regulation and quality controls. Ribosome-interacting factors are critical for the quality control mechanisms responding to abnormal translation arrest by targeting its products for degradation. Aberrant mRNAs are produced by errors in mRNA maturation steps and cause aberrant translation and are eliminated by the quality control system. In this review, we focus on recent progress on two quality controls, Ribosome-associated Quality Control (RQC) and No-Go Decay (NGD), for abnormal translational elongation. These quality controls recognize aberrant ribosome stalling and induce rapid degradation of aberrant polypeptides and mRNAs thereby maintaining protein homeostasis and preventing the protein aggregation.
  • Toshiaki Izawa, Sae-Hun Park, Liang Zhao, F. Ulrich Hartl, Walter Neupert
    CELL 171(4) 890-+ 2017年11月  査読有り
    Eukaryotic cells have evolved extensive protein quality-control mechanisms to remove faulty translation products. Here, we show that yeast cells continually produce faulty mitochondrial polypeptides that stall on the ribosome during translation but are imported into the mitochondria. The cytosolic protein Vms1, together with the E3 ligase Ltn1, protects against the mitochondrial toxicity of these proteins and maintains cell viability under respiratory conditions. In the absence of these factors, stalled polypeptides aggregate after import and sequester critical mitochondrial chaperone and translation machinery. Aggregation depends on C-terminal alanyl/threonyl sequences (CAT-tails) that are attached to stalled polypeptides on 60S ribosomes by Rqc2. Vms1 binds to 60S ribosomes at the mitochondrial surface and antagonizes Rqc2, thereby facilitating import, impeding aggregation, and directing aberrant polypeptides to intra-mitochondrial quality control. Vms1 is a key component of a rescue pathway for ribosome-stalled mitochondrial polypeptides that are inaccessible to ubiquitylation due to coupling of translation and translocation.

MISC

 8

書籍等出版物

 2

共同研究・競争的資金等の研究課題

 1