Evidence map›Paper›PMID 24778241›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Endophilin A1 induces different membrane shapes using a conformational switch that is regulated by phosphorylation.

Mark R Ambroso, Balachandra G Hegde, Ralf Langen

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed.

  1. Article
  2. Review
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  4. Article
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  6. Article
  7. Review
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  9. Article
  10. Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Presynaptic Autophagy and the Connection With Neurotransmission.Frontiers in cell and developmental biology · 2021
    Review
  19. Dysfunction of Synaptic Vesicle Endocytosis in Parkinson's Disease.Frontiers in integrative neuroscience · 2021
    Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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

3 authors.

Mark R AmbrosoDepartment of Biochemistry and Molecular Biology, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033.
Balachandra G HegdeDepartment of Biochemistry and Molecular Biology, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033.
Ralf LangenDepartment of Biochemistry and Molecular Biology, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033 Langen@usc.edu.

Funding

Structural Analysis of Protein-Membrane InteractionR01GM063915 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2001 to 2012
$2.8M
NIGMS NIH HHS GM063915NIGMS NIH HHS R01 GM063915
6 · The paper itself

Abstract

Membrane remodeling is controlled by proteins that can promote the formation of highly curved spherical or cylindrical membranes. How a protein induces these different types of membrane curvature and how cells regulate this process is still unclear. Endophilin A1 is a protein involved in generating endocytotic necks and vesicles during synaptic endocytosis and can transform large vesicles into lipid tubes or small and highly curved vesicles in vitro. By using EM and electron paramagnetic resonance of endophilin A1, we find that tubes are formed by a close interaction with endophilin A1's BIN/amphiphysin/Rvs (BAR) domain and deep insertion of its amphipathic helices. In contrast, vesicles are predominantly stabilized by the shallow insertion of the amphipathic helical wedges with the BAR domain removed from the membrane. By showing that the mechanism of membrane curvature induction is different for vesiculation and tubulation, these data also explain why previous studies arrived at different conclusions with respect to the importance of scaffolding and wedging in the membrane curvature generation of BAR proteins. The Parkinson disease-associated kinase LRRK2 phosphorylates S75 of endophilin A1, a position located in the acyl chain region on tubes and the aqueous environment on vesicles. We find that the phosphomimetic mutation S75D favors vesicle formation by inhibiting this conformational switch, acting to regulate endophilin A1-mediated curvature. As endophilin A1 is part of a protein superfamily, we expect these mechanisms and their regulation by posttranslational modifications to be a general means for controlling different types of membrane curvature in a wide range of processes in vivo.

Indexed as

AcyltransferasesAnimalsCrystallography, X-RayDimerizationElectronsHumansLipidsLiposomesMembrane ProteinsPhosphorylationProtein Structure, SecondaryProtein Structure, TertiaryRatsSpin LabelsStructure-Activity Relationship2-acylglycerophosphate acyltransferaseAcyltransferasesLipidsLiposomesMembrane ProteinsSpin Labelsdouble electron–electron resonancesite-directed spin labeling

Identifiers

PMID24778241
PMCPMC4024918

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.