Evidence map›Paper›PMID 18779371›Full record

ArticleThe Journal of cell biology2008

To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology.

Mikhail Bogdanov, Jun Xie, Phil Heacock, William Dowhan

Abstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing 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

78 citing papers in PubMed.

  1. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
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18 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

4 authors.

Mikhail BogdanovDepartment of Biochemistry and Molecular Biology, University of Texas-Houston Medical School and Graduate School of Biomedical Sciences, Houston, TX 77225, USA.
Jun Xie
Phil Heacock
William Dowhan

Funding

Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
NIGMS NIH HHS R37 GM020478NIGMS NIH HHS R37 GM20478
6 · The paper itself

Abstract

The molecular details of how lipids influence final topological organization of membrane proteins are not well understood. Here, we present evidence that final topology is influenced by lipid-protein interactions most likely outside of the translocon. The N-terminal half of Escherichia coli lactose permease (LacY) is inverted with respect to the C-terminal half and the membrane bilayer when assembled in mutants lacking phosphatidylethanolamine and containing only negatively charged phospholipids. We demonstrate that inversion is dependent on interactions between the net charge of the cytoplasmic surface of the N-terminal bundle and the negative charge density of the membrane bilayer surface. A transmembrane domain, acting as a molecular hinge between the two halves of the protein, must also exit from the membrane for inversion to occur. Phosphatidylethanolamine dampens the translocation potential of negative residues in favor of the cytoplasmic retention potential of positive residues, thus explaining the dominance of positive over negative amino acids as co- or post-translational topological determinants.

Indexed as

Escherichia coliEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsMembrane LipidsMembrane ProteinsModels, MolecularMonosaccharide Transport ProteinsPhosphatidylethanolaminesProtein Structure, TertiarySymportersEscherichia coli ProteinsLacY protein, E coliMembrane LipidsMembrane ProteinsMonosaccharide Transport ProteinsphosphatidylethanolaminePhosphatidylethanolaminesSymporters

Identifiers

PMID18779371
PMCPMC2528571

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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.