Evidence map›Paper›PMID 23133367›Full record

ArticlePLoS computational biology2012

Structural insights into the inhibition of actin-capping protein by interactions with phosphatidic acid and phosphatidylinositol (4,5)-bisphosphate.

Roman Pleskot, Přemysl Pejchar, Viktor Žárský, Christopher J Staiger, Martin Potocký

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2012. 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
2.5field-weighted citation impact, top 11% 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, 46 citations in OpenAlex.

  1. Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024
    Review
  2. Review
  3. Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  9. Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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 4 institutions in 2 countries.

Roman PleskotInstitute of Experimental Botany, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Přemysl Pejchar
Viktor Žárský
Christopher J Staiger
Martin Potocký
Czech Academy of Sciences, Institute of Experimental Botany · CZCharles University · CZCzech Academy of Sciences · CZPurdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin cytoskeleton is a dynamic structure that coordinates numerous fundamental processes in eukaryotic cells. Dozens of actin-binding proteins are known to be involved in the regulation of actin filament organization or turnover and many of these are stimulus-response regulators of phospholipid signaling. One of these proteins is the heterodimeric actin-capping protein (CP) which binds the barbed end of actin filaments with high affinity and inhibits both addition and loss of actin monomers at this end. The ability of CP to bind filaments is regulated by signaling phospholipids, which inhibit the activity of CP; however, the exact mechanism of this regulation and the residues on CP responsible for lipid interactions is not fully resolved. Here, we focus on the interaction of CP with two signaling phospholipids, phosphatidic acid (PA) and phosphatidylinositol (4,5)-bisphosphate (PIP(2)). Using different methods of computational biology such as homology modeling, molecular docking and coarse-grained molecular dynamics, we uncovered specific modes of high affinity interaction between membranes containing PA/phosphatidylcholine (PC) and plant CP, as well as between PIP(2)/PC and animal CP. In particular, we identified differences in the binding of membrane lipids by animal and plant CP, explaining previously published experimental results. Furthermore, we pinpoint the critical importance of the C-terminal part of plant CPα subunit for CP-membrane interactions. We prepared a GST-fusion protein for the C-terminal domain of plant α subunit and verified this hypothesis with lipid-binding assays in vitro.

Indexed as

Actin Capping ProteinsAmino Acid SequenceAnimalsArabidopsis ProteinsAvian ProteinsChickensComputational BiologyHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Sequence DataMutationPhosphatidic AcidsPhosphatidylinositol PhosphatesPhylogenyProtein BindingSequence AlignmentActin Capping ProteinsArabidopsis ProteinsAvian ProteinsPhosphatidic AcidsPhosphatidylinositol Phosphates

Identifiers

PMID23133367
PMCPMC3486809
OpenAlexW2146041950

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.