Evidence map›Paper›PMID 22522801›Full record

ArticleProteomics2012

Multiple phosphorylations of cytochrome c oxidase and their functions.

Stefan Helling, Maik Hüttemann, Rabia Ramzan, Su Hyeon Kim, Icksoo Lee, Thorsten Müller, Elmar Langenfeld, Helmut E Meyer, Bernhard Kadenbach, Sebastian Vogt and 1 more

Abstract read
In one paragraph

Article in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Interaction of Terminal Oxidases with Amphipathic Molecules.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Structures ofScience (New York, N.Y.) · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Serine-47 phosphorylation of cytochromeFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  14. Article
  15. Review
  16. Article
  17. 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

11 authors.

Stefan HellingMedizinisches Proteom-Center, Funktionelle Proteomik, Ruhr-Universität Bochum, Bochum, Germany.
Maik Hüttemann
Rabia Ramzan
Su Hyeon Kim
Icksoo Lee
Thorsten Müller
Elmar Langenfeld
Helmut E Meyer
Bernhard Kadenbach
Sebastian Vogt
Katrin Marcus

Funding

Regulation of Respiration and Apoptosis by Cytochrome c Phosphorylation.R01GM089900 · NIGMS · WAYNE STATE UNIVERSITY · PI HUETTEMANN, MAIK · 2010 to 2014
$1.4M
NIGMS NIH HHS GM089900NIGMS NIH HHS R01 GM089900
6 · The paper itself

Abstract

Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial electron transport chain, is regulated by isozyme expression, allosteric effectors such as the ATP/ADP ratio, and reversible phosphorylation. Of particular interest is the "allosteric ATP-inhibition," which has been hypothesized to keep the mitochondrial membrane potential at low healthy values (<140 mV), thus preventing the formation of superoxide radical anions, which have been implicated in multiple degenerative diseases. It has been proposed that the "allosteric ATP-inhibition" is switched on by the protein kinase A-dependent phosphorylation of COX. The goal of this study was to identify the phosphorylation site(s) involved in the "allosteric ATP-inhibition" of COX. We report the mass spectrometric identification of four new phosphorylation sites in bovine heart COX. The identified phosphorylation sites include Tyr-218 in subunit II, Ser-1 in subunit Va, Ser-2 in subunit Vb, and Ser-1 in subunit VIIc. With the exception of Ser-2 in subunit Vb, the identified phosphorylation sites were found in enzyme samples with and without "allosteric ATP inhibition," making Ser-2 of subunit Vb a candidate site enabling allosteric regulation. We therefore hypothesize that additional phosphorylation(s) may be required for the "allosteric ATP-inhibition," and that these sites may be easily dephosphorylated or difficult to identify by mass spectrometry.

Indexed as

Allosteric RegulationAmino Acid SequenceAnimalsCattleChromatography, High Pressure LiquidElectron Transport Complex IVMolecular Sequence DataMyocardiumPhosphopeptidesPhosphorylationProtein SubunitsTandem Mass SpectrometryElectron Transport Complex IVPhosphopeptidesProtein Subunits

Identifiers

PMID22522801
PMCPMC3728716

What OpenQuestion holds

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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.