English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis

Izawa, T., Park, S.-H., Zhao, L., Hartl, F. U., & Neupert, W. (2017). Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis. Cell, 171(4), 890-903. doi:10.1016/j.cell.2017.10.002.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Izawa, Toshiaki1, Author              
Park, Sae-Hun2, Author              
Zhao, Liang2, Author              
Hartl, F. Ulrich2, Author              
Neupert, Walter1, Author              
Affiliations:
1Neupert, Walter / Structure and Function of Mitochondria, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565163              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

Content

show
hide
Free keywords: SACCHAROMYCES-CEREVISIAE; CONTROL COMPLEX; FLUORESCENT PROTEINS; YEAST GENES; STRESS; QUANTIFICATION; DEGRADATION; AGGREGATION; PROTEOMICS; CLEARANCEBiochemistry & Molecular Biology; Cell Biology;
 Abstract: 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.

Details

show
hide
Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: 24
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show hide
Project name : FP7 GA no. ERC-2012-SyG_318987 – ToPAG
Grant ID : 318987
Funding program : Funding Programme 7 (FP7)
Funding organization : European Commission (EC)

Source 1

show
hide
Title: Cell
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 171 (4) Sequence Number: - Start / End Page: 890 - 903 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183