Evidence map›Paper›PMID 27974465›Full record

ArticleThe Journal of biological chemistry2017

Dynamic Lipid-dependent Modulation of Protein Topology by Post-translational Phosphorylation.

Heidi Vitrac, David M MacLean, Anja Karlstaedt, Heinrich Taegtmeyer, Vasanthi Jayaraman, Mikhail Bogdanov, William Dowhan

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Structure and function ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  12. Review
  13. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  14. Membranes as the third genetic code.Molecular biology reports · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

7 authors.

Heidi VitracFrom the Department of Biochemistry and Molecular Biology and Center for Membrane Biology, University of Texas McGovern Medical School, Houston, Texas 77030. Electronic address: Heidi.Vitrac@uth.tmc.edu.
David M MacLeanFrom the Department of Biochemistry and Molecular Biology and Center for Membrane Biology, University of Texas McGovern Medical School, Houston, Texas 77030.
Anja Karlstaedtthe Department of Internal Medicine, Division of Cardiology, University of Texas McGovern Medical School, Houston, Texas 77030.
Heinrich Taegtmeyerthe Department of Internal Medicine, Division of Cardiology, University of Texas McGovern Medical School, Houston, Texas 77030.
Vasanthi JayaramanFrom the Department of Biochemistry and Molecular Biology and Center for Membrane Biology, University of Texas McGovern Medical School, Houston, Texas 77030.
Mikhail BogdanovFrom the Department of Biochemistry and Molecular Biology and Center for Membrane Biology, University of Texas McGovern Medical School, Houston, Texas 77030.
William DowhanFrom the Department of Biochemistry and Molecular Biology and Center for Membrane Biology, University of Texas McGovern Medical School, Houston, Texas 77030. Electronic address: william.dowhan@uth.tmc.edu.

Funding

SWITCHING OF METABOLIC GENES IN UNLOADED HEARTR01HL061483 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI TAEGTMEYER, HEINRICH · 1999 to 2021
$6.2M
Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
Structure and Function of NMDA ReceptorsR01GM094246 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2011 to 2016
$2.0M
TARP modulation of AMPA receptorsR01GM113212 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAYARAMAN, VASANTHI · 2015 to 2017
$897k
3D structure and function of Acid Sensing Ion channelsK99NS094761 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MACLEAN, DAVID MALCOM · 2015 to 2016
$173k
NHLBI NIH HHS R01 HL061483NIGMS NIH HHS R01 GM094246NIGMS NIH HHS R01 GM113212NIGMS NIH HHS R37 GM020478NINDS NIH HHS K99 NS094761
6 · The paper itself

Abstract

Membrane protein topology and folding are governed by structural principles and topogenic signals that are recognized and decoded by the protein insertion and translocation machineries at the time of initial membrane insertion and folding. We previously demonstrated that the lipid environment is also a determinant of initial protein topology, which is dynamically responsive to post-assembly changes in membrane lipid composition. However, the effect on protein topology of post-assembly phosphorylation of amino acids localized within initially cytoplasmically oriented extramembrane domains has never been investigated. Here, we show in a controlled in vitro system that phosphorylation of a membrane protein can trigger a change in topological arrangement. The rate of change occurred on a scale of seconds, comparable with the rates observed upon changes in the protein lipid environment. The rate and extent of topological rearrangement were dependent on the charges of extramembrane domains and the lipid bilayer surface. Using model membranes mimicking the lipid compositions of eukaryotic organelles, we determined that anionic lipids, cholesterol, sphingomyelin, and membrane fluidity play critical roles in these processes. Our results demonstrate how post-translational modifications may influence membrane protein topology in a lipid-dependent manner, both along the organelle trafficking pathway and at their final destination. The results provide further evidence that membrane protein topology is dynamic, integrating for the first time the effect of changes in lipid composition and regulators of cellular processes. The discovery of a new topology regulatory mechanism opens additional avenues for understanding unexplored structure-function relationships and the development of optimized topology prediction tools.

Indexed as

Protein Processing, Post-TranslationalCell MembraneLipid BilayersMembrane LipidsMembrane ProteinsPhosphorylationProtein DomainsLipid BilayersMembrane LipidsMembrane Proteinsfluorescence resonance energy transfer (FRET)glycerophospholipidlipid-protein interactionmembrane proteinphosphorylationpost-translational modification (PTM)

Identifiers

PMID27974465
PMCPMC5290939

What OpenQuestion holds

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Registered trials

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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.