Evidence map›Paper›PMID 18719119›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting.

Jörg Balss, Panagiotis Papatheodorou, Mario Mehmel, Dirk Baumeister, Brigitte Hertel, Nicolas Delaroque, Franck C Chatelain, Daniel L Minor, James L Van Etten, Joachim Rassow and 2 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. A Functional KViruses · 2020
    Article
  5. Chloroviruses.Viruses · 2019
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Physiology of potassium channels in the inner membrane of mitochondria.Pflugers Archiv : European journal of physiology · 2012
    Review
  17. Chloroviruses: not your everyday plant virus.Trends in plant science · 2012
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Jörg BalssInstitute of Botany, Technische Universität Darmstadt, D-64287 Darmstadt, Germany.
Panagiotis Papatheodorou
Mario Mehmel
Dirk Baumeister
Brigitte Hertel
Nicolas Delaroque
Franck C Chatelain
Daniel L Minor
James L Van Etten
Joachim Rassow
Anna Moroni
Gerhard Thiel

Funding

VIRAL SHUTOFF OF HOST TRANSCRIPTION--PBCV-1 INFECTEDP20RR015635 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2000 to 2009
$22.1M
GENOME AND GENETICS OF A EUKARYOTIC ALGAL VIRUSR01GM032441 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI VAN ETTEN, JAMES L · 1985 to 2009
$2.8M
NCRR NIH HHS P20 RR015635NCRR NIH HHS P21RR15635NIGMS NIH HHS GM32441NIGMS NIH HHS R01 GM032441
6 · The paper itself

Abstract

K(+) channels operate in the plasma membrane and in membranes of organelles including mitochondria. The mechanisms and topogenic information for their differential synthesis and targeting is unknown. This article describes 2 similar viral K(+) channels that are differentially sorted; one protein (Kesv) is imported by the Tom complex into the mitochondria, the other (Kcv) to the plasma membrane. By creating chimeras we discovered that mitochondrial sorting of Kesv depends on a hierarchical combination of N- and C-terminal signals. Crucial is the length of the second transmembrane domain; extending its C terminus by > or = 2 hydrophobic amino acids redirects Kesv from the mitochondrial to the plasma membrane. Activity of Kesv in the plasma membrane is detected electrically or by yeast rescue assays only after this shift in sorting. Hence only minor structural alterations in a transmembrane domain are sufficient to switch sorting of a K(+) channel between the plasma membrane and mitochondria.

Indexed as

Protein Sorting SignalsAmino Acid SequenceCell LineCell MembraneHumansMembrane ProteinsMitochondriaMutagenesis, Site-DirectedPhycodnaviridaePotassium ChannelsProtein TransportSaccharomyces cerevisiaeTransfectionViral ProteinsMembrane ProteinsPotassium ChannelsProtein Sorting SignalsViral Proteins

Identifiers

PMID18719119
PMCPMC2518832

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.