Evidence map›Paper›PMID 34753925›Full record

ArticleNature communications2021

Lysine acetylation regulates the interaction between proteins and membranes.

Alan K Okada, Kazuki Teranishi, Mark R Ambroso, Jose Mario Isas, Elena Vazquez-Sarandeses, Joo-Yeun Lee, Arthur Alves Melo, Priyatama Pandey, Daniel Merken, Leona Berndt and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
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

41 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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  7. Review
  8. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Regulation of mNature plants · 2025
    Article
  14. Deciphering the language of mingling lipids and proteins.Current opinion in structural biology · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Activity-Based Acylome Profiling withJournal of the American Chemical Society · 2024
    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

15 authors at 4 institutions in 2 countries.

Alan K Okada *Regions Hospital Department of Emergency Medicine, Saint Paul, MN, 55101, USA.ORCID 0000-0001-8338-9557
Kazuki Teranishi *Zilkha Neurogenetic Institute, Department of Physiology and Neuroscience, University of Southern California, Los Angeles, CA, 90033, USA.
Mark R Ambroso *Zilkha Neurogenetic Institute, Department of Physiology and Neuroscience, University of Southern California, Los Angeles, CA, 90033, USA.
Jose Mario IsasZilkha Neurogenetic Institute, Department of Physiology and Neuroscience, University of Southern California, Los Angeles, CA, 90033, USA.
Elena Vazquez-SarandesesMax-Delbrück-Center for Molecular Medicine, Crystallography, Robert-Rössle-Straße 10, 13092, Berlin, Germany.
Joo-Yeun LeeNeuroscience Graduate Program, University of Southern California, Los Angeles, CA, USA.ORCID 0000-0001-6616-5594
Arthur Alves MeloMax-Delbrück-Center for Molecular Medicine, Crystallography, Robert-Rössle-Straße 10, 13092, Berlin, Germany.
Priyatama PandeyDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA, 90089, USA.
Daniel MerkenDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA, 90089, USA.
Leona BerndtInstitute for Biochemistry, Synthetic and Structural Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Michael LammersInstitute for Biochemistry, Synthetic and Structural Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Oliver DaumkeMax-Delbrück-Center for Molecular Medicine, Crystallography, Robert-Rössle-Straße 10, 13092, Berlin, Germany.ORCID 0000-0002-6190-1414
Karen ChangZilkha Neurogenetic Institute, Department of Physiology and Neuroscience, University of Southern California, Los Angeles, CA, 90033, USA.
Ian S HaworthDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA, 90089, USA.ORCID 0000-0002-3873-0899
Ralf LangenZilkha Neurogenetic Institute, Department of Physiology and Neuroscience, University of Southern California, Los Angeles, CA, 90033, USA. Langen@usc.edu.
University of Southern California · USMax Delbrück Center · DEUniversität Greifswald · DERegions Hospital · US

Funding

Molecular mechanisms of huntingtin misfoldingR01NS084345 · NINDS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2015 to 2019
$2.2M
Membrane remodeling by alpha-synuclein: implications for function and diseaseR01GM115736 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2015 to 2018
$1.3M
NIGMS NIH HHS R01 GM115736NINDS NIH HHS R01 NS084345
6 · The paper itself

Abstract

Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates membrane protein function. Here, we use bioinformatics, biophysical analysis of recombinant proteins, live-cell fluorescent imaging and genetic manipulation of Drosophila to explore lysine acetylation in peripheral membrane proteins. Analysis of 50 peripheral membrane proteins harboring BAR, PX, C2, or EHD membrane-binding domains reveals that lysine acetylation predominates in membrane-interaction regions. Acetylation and acetylation-mimicking mutations in three test proteins, amphiphysin, EHD2, and synaptotagmin1, strongly reduce membrane binding affinity, attenuate membrane remodeling in vitro and alter subcellular localization. This effect is likely due to the loss of positive charge, which weakens interactions with negatively charged membranes. In Drosophila, acetylation-mimicking mutations of amphiphysin cause severe disruption of T-tubule organization and yield a flightless phenotype. Our data provide mechanistic insights into how lysine acetylation regulates membrane protein function, potentially impacting a plethora of membrane-related processes.

Indexed as

AcetylationAnimalsDrosophilaLysineMutationNerve Tissue ProteinsamphiphysinLysineNerve Tissue Proteins

Identifiers

PMID34753925
PMCPMC8578602
OpenAlexW3214408574

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.