Evidence map›Paper›PMID 16698795›Full record

ArticleThe Journal of biological chemistry2006

Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease.

Jun Xie, Mikhail Bogdanov, Philip Heacock, William Dowhan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
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  8. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
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  19. Charge asymmetry in the proteins of the outer membrane.Bioinformatics (Oxford, England) · 2013
    Article
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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

4 authors at 1 institution in 1 country.

Jun XieDepartment of Biochemistry and Molecular Biology, University of Texas-Houston, Medical School, 77030, USA.
Mikhail Bogdanov
Philip Heacock
William Dowhan
The University of Texas Health Science Center at Houston · US

Funding

Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
STRUCTURE/FUNCTION OF MEMBRANE PROTEINSR01GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 1985 to 2004
$1.8M
NIGMS NIH HHS R01 GM020478NIGMS NIH HHS R37 GM020478NIGMS NIH HHS R37 GM20478
6 · The paper itself

Abstract

To determine the specific role lipids play in membrane protein topogenesis in vivo, the orientation with respect to the membrane bilayer of Escherichia coli lactose permease (LacY) transmembrane (TM) domains and their flanking extramembrane domains was compared after assembly in native membranes and membranes with genetically modified lipid content using the substituted cysteine accessibility method for determining TM domain mapping. LacY assembled in the absence of the major membrane lipid phosphatidylethanolamine (PE) does not carry out uphill transport of substrate and displays an inverted orientation for the N-terminal six-TM domain helical bundle (Bogdanov, M., Heacock, P. N., and Dowhan, W. (2002) EMBO J. 21, 2107-2116). Strikingly, the replacement of PE in vivo by the foreign lipid monoglucosyldiacylglycerol (MGlcDAG), synthesized by the Acholeplasma laidlawii MGlcDAG synthase, restored uphill transport and supported the wild type TM topology of the N-terminal helical bundle of LacY. An interchangeable role in defining membrane protein TM domain orientation and supporting function is played by the two most abundant lipids, PE and MGlcDAG, in gram-negative and gram-positive bacteria, respectively. Therefore, these structurally diverse lipids endow the membrane with similar properties necessary for the proper organization of protein domains in LacY that are highly sensitive to lipids as topological determinants.

Indexed as

Cell MembraneCysteineEscherichia coliEscherichia coli ProteinsGlycolipidsLipid MetabolismLipidsMembrane ProteinsMembrane Transport ProteinsMonosaccharide Transport ProteinsPhosphatidylethanolaminesProtein Structure, TertiarySymportersCysteineEscherichia coli Proteinsglucosyl diacylglycerolGlycolipidslactose permeaseLacY protein, E coliLipidsMembrane ProteinsMembrane Transport ProteinsMonosaccharide Transport ProteinsphosphatidylethanolaminePhosphatidylethanolaminesSymporters

Identifiers

PMID16698795
PMCPMC4082682
OpenAlexW1999726178

What OpenQuestion holds

Textmetadata
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.