Evidence map›Paper›PMID 27956138›Full record

ReviewBiochimica et biophysica acta. Molecular and cell biology of lipids2017

Biogenesis, transport and remodeling of lysophospholipids in Gram-negative bacteria.

Lei Zheng, Yibin Lin, Shuo Lu, Jiazhe Zhang, Mikhail Bogdanov

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

57 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  5. Lipidome Disturbances ofMicroorganisms · 2026
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  13. Review
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  15. Structural basis for surface activation of the classical complement cascade by the short pentraxin C-reactive protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. TheJournal of bacteriology · 2024
    Article
  18. A periplasmic phospholipase that maintains outer membrane lipid asymmetry inProceedings of the National Academy of Sciences of the United States of America · 2023
    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

5 authors at 2 institutions in 1 country.

Lei ZhengCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA. Electronic address: lei.zheng@uth.tmc.edu.
Yibin LinCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
Shuo LuCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
Jiazhe ZhangCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
Mikhail BogdanovDepartment of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston McGovern Medical School, 6431 Fannin Street, Houston, TX 77030, USA.
The University of Texas Health Science Center at Houston · USThe University of Texas Health Science Center · US

Funding

Phospholipid Metabolism in Cell MembraneR01GM098572 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHENG, LEI · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM098572
6 · The paper itself

Abstract

Lysophospholipids (LPLs) are metabolic intermediates in bacterial phospholipid turnover. Distinct from their diacyl counterparts, these inverted cone-shaped molecules share physical characteristics of detergents, enabling modification of local membrane properties such as curvature. The functions of LPLs as cellular growth factors or potent lipid mediators have been extensively demonstrated in eukaryotic cells but are still undefined in bacteria. In the envelope of Gram-negative bacteria, LPLs are derived from multiple endogenous and exogenous sources. Although several flippases that move non-glycerophospholipids across the bacterial inner membrane were characterized, lysophospholipid transporter LplT appears to be the first example of a bacterial protein capable of facilitating rapid retrograde translocation of lyso forms of glycerophospholipids across the cytoplasmic membrane in Gram-negative bacteria. LplT transports lyso forms of the three bacterial membrane phospholipids with comparable efficiency, but excludes other lysolipid species. Once a LPL is flipped by LplT to the cytoplasmic side of the inner membrane, its diacyl form is effectively regenerated by the action of a peripheral enzyme, acyl-ACP synthetase/LPL acyltransferase (Aas). LplT-Aas also mediates a novel cardiolipin remodeling by converting its two lyso derivatives, diacyl or deacylated cardiolipin, to a triacyl form. This coupled remodeling system provides a unique bacterial membrane phospholipid repair mechanism. Strict selectivity of LplT for lyso lipids allows this system to fulfill efficient lipid repair in an environment containing mostly diacyl phospholipids. A rocker-switch model engaged by a pair of symmetric ion-locks may facilitate alternating substrate access to drive LPL flipping into bacterial cells. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.

Indexed as

LipogenesisBacterial ProteinsBiological TransportCarbon-Sulfur LigasesCell WallGram-Negative BacteriaLysophospholipidsPhospholipid Transfer ProteinsSignal TransductionSubstrate SpecificityBacterial ProteinsCarbon-Sulfur Ligaseslong-chain-fatty-acid-(acyl-carrier-protein) ligaseLysophospholipidsPhospholipid Transfer ProteinsBacterial lipidFlippaseLplTLysophospholipidMembraneRemodeling

Identifiers

PMID27956138
PMCPMC6162059
OpenAlexW2560752408

What OpenQuestion holds

Textmetadata
LicenceTDM
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.