English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Quality control of nonstop membrane proteins at the ER membrane and in the cytosol

Arakawa, S., Yunoki, K., Izawa, T., Tamura, Y., Nishikawa, S.-i., & Endo, T. (2016). Quality control of nonstop membrane proteins at the ER membrane and in the cytosol. Scientific Reports, 6: 30795. doi:10.1038/srep30795.

Item is

Files

show Files
hide Files
:
srep30795.pdf (Publisher version), 2MB
Name:
srep30795.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
This work is licensed under a Creative Commons Attribution 4.0 International License.
License:
-
:
srep30795-s1.pdf (Supplementary material), 299KB
Name:
srep30795-s1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Arakawa, Shunsuke1, Author
Yunoki, Kaori1, Author
Izawa, Toshiaki2, Author              
Tamura, Yasushi1, Author
Nishikawa, Shuh-ichi1, Author
Endo, Toshiya1, Author
Affiliations:
1external, ou_persistent22              
2Neupert, Walter / Structure and Function of Mitochondria, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565163              

Content

show
hide
Free keywords: ENDOPLASMIC-RETICULUM MEMBRANE; MESSENGER-RNA; SACCHAROMYCES-CEREVISIAE; UBIQUITIN LIGASE; CONTROL SYSTEMS; RIBOSOME; TRANSLOCATION; TERMINATION; SIGNAL; DISSOCIATIONScience & Technology - Other Topics;
 Abstract: Since messenger RNAs without a stop codon (nonstop mRNAs) for organelle-targeted proteins and their translation products (nonstop proteins) generate clogged translocon channels as well as stalled ribosomes, cells have mechanisms to degrade nonstop mRNAs and nonstop proteins and to clear the translocons (e.g. the Sec61 complex) by release of nonstop proteins into the organellar lumen. Here we followed the fate of nonstop endoplasmic reticulum (ER) membrane proteins with different membrane topologies in yeast to evaluate the importance of the Ltn1-dependent cytosolic degradation and the Dom34-dependent release of the nonstop membrane proteins. Ltn1-dependent degradation differed for membrane proteins with different topologies and its failure did not affect ER protein import or cell growth. On the other hand, failure in the Dom34-dependent release of the nascent polypeptide from the ribosome led to the block of the Sec61 channel and resultant inhibition of other protein import into the ER caused cell growth defects. Therefore, the nascent chain release from the translation apparatus is more instrumental in clearance of the clogged ER translocon channel and thus maintenance of normal cellular functions.

Details

show
hide
Language(s): eng - English
 Dates: 2016-03-072016-07-112016-08-02
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000380636200001
DOI: 10.1038/srep30795
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 6 Sequence Number: 30795 Start / End Page: - Identifier: Other: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322