Evidence map›Paper›PMID 31445680›Full record

ArticleBiophysical journal2019

PIP2 Reshapes Membranes through Asymmetric Desorption.

Sankalp Shukla, Rui Jin, Jaclyn Robustelli, Zachary E Zimmerman, Tobias Baumgart

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Regulation of ThermoTRP Channels by PIP2 and Cholesterol.Advances in experimental medicine and biology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  18. Membrane Heterogeneity Controls Cellular Endocytic Trafficking.Frontiers in cell and developmental biology · 2020
    Review
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

5 authors at 1 institution in 1 country.

Sankalp ShuklaDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania.
Rui JinDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania.
Jaclyn RobustelliDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania.
Zachary E ZimmermanDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania.
Tobias BaumgartDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania. Electronic address: baumgart@sas.upenn.edu.
University of Pennsylvania · US

Funding

PSOC@Penn Education and OutreachU54CA193417 · NCI · UNIVERSITY OF PENNSYLVANIA · PI DISCHER, DENNIS E. · 2015 to 2020
$10.5M
Membrane shape transition control in cellular membrane trafficking phenomenaR01GM097552 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BAUMGART, TOBIAS · 2011 to 2023
$4.5M
NCI NIH HHS U54 CA193417NIGMS NIH HHS R01 GM097552
6 · The paper itself

Abstract

Phosphatidylinositol-4,5-bisphosphate (PIP2) is an important signaling lipid in eukaryotic cell plasma membranes, playing an essential role in diverse cellular processes. The headgroup of PIP2 is highly negatively charged, and this lipid displays a high critical micellar concentration compared to housekeeping phospholipid analogs. Given the crucial role of PIP2, it is imperative to study its localization, interaction with proteins, and membrane-shaping properties. Biomimetic membranes have served extensively to elucidate structural and functional aspects of cell membranes including protein-lipid and lipid-lipid interactions, as well as membrane mechanics. Incorporation of PIP2 into biomimetic membranes, however, has at times resulted in discrepant findings described in the literature. With the goal to elucidate the mechanical consequences of PIP2 incorporation, we studied the desorption of PIP2 from biomimetic giant unilamellar vesicles by means of a fluorescent marker. A decrease in fluorescence intensity with the age of the vesicles suggested that PIP2 lipids were being desorbed from the outer leaflet of the membrane. To evaluate whether this desorption was asymmetric, the vesicles were systematically diluted. This resulted in an increase in the number of internally tubulated vesicles within minutes after dilution, suggesting that the desorption was asymmetric and also generated membrane curvature. By means of a saturated chain homolog of PIP2, we showed that the fast desorption of PIP2 is facilitated by presence of an arachidonic lipid tail and is possibly due to its oxidation. Through measurements of the pulling force of membrane tethers, we quantified the effect of this asymmetric desorption on the spontaneous membrane curvature. Furthermore, we found that the spontaneous curvature could be modulated by externally increasing the concentration of PIP2 micelles. Given that the local concentration of PIP2 in biological membranes is variable, spontaneous curvature generated by PIP2 may affect the formation of highly curved structures that can serve as initiators for signaling events.

Indexed as

AnimalsCell MembraneHumansMicellesPhosphatidylinositol 4,5-DiphosphateSwineMicellesPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID31445680
PMCPMC6731468
OpenAlexW2965584683

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.