Evidence map›Paper›PMID 22619173›Full record

ArticleThe Journal of biological chemistry2012

Hydrophobic matching controls the tilt and stability of the dimeric platelet-derived growth factor receptor (PDGFR) β transmembrane segment.

Claudia Muhle-Goll, Silke Hoffmann, Sergii Afonin, Stephan L Grage, Anton A Polyansky, Dirk Windisch, Marcel Zeitler, Jochen Bürck, Anne S Ulrich

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 65 citations in OpenAlex.

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  7. Structural and functional characterization of the pore-forming domain of pinholin SProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Active SBiochimica et biophysica acta. Biomembranes · 2020
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  9. Review
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  14. Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation.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

9 authors at 2 institutions in 3 countries.

Claudia Muhle-GollInstitute for Biological Interfaces (IBG-2), Karlsruhe Institute of Technology, P. O. Box 3640, 76021 Karlsruhe, Germany.
Silke Hoffmann
Sergii Afonin
Stephan L Grage
Anton A Polyansky
Dirk Windisch
Marcel Zeitler
Jochen Bürck
Anne S Ulrich
Karlsruhe Institute of Technology · DEInstitute of Bioorganic Chemistry · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The platelet-derived growth factor receptor β is a member of the cell surface receptor tyrosine kinase family and dimerizes upon activation. We determined the structure of the transmembrane segment in dodecylphosphocholine micelles by liquid-state NMR and found that it forms a stable left-handed helical dimer. Solid-state NMR and oriented circular dichroism were used to measure the tilt angle of the helical segments in macroscopically aligned model membranes with different acyl chain lengths. Both methods showed that decreasing bilayer thickness (DEPC-POPC-DMPC) led to an increase in the helix tilt angle from 10° to 30° with respect to the bilayer normal. At the same time, reconstitution of the comparatively long hydrophobic segment became less effective, eventually resulting in complete protein aggregation in the short-chain lipid DLPC. Unrestrained molecular dynamics simulations of the dimer were carried out in explicit lipid bilayers (DEPC, POPC, DMPC, sphingomyelin), confirming the observed dependence of the helix tilt angle on bilayer thickness. Notably, molecular dynamics revealed that the left-handed dimer gets tilted en bloc, whereas conformational transitions to alternative (e.g. right-handed dimeric) states were not supported. The experimental data along with the simulation results demonstrate a pronounced interplay between the platelet-directed growth factor receptor β transmembrane segment and the bilayer thickness. The effect of hydrophobic mismatch might play a key role in the redistribution and activation of the receptor within different lipid microdomains of the plasma membrane in vivo.

Indexed as

Circular DichroismCross-Linking ReagentsHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMicellesMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein MultimerizationProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryReceptor, Platelet-Derived Growth Factor betaSuccinimidesbis(sulfosuccinimidyl)suberateCross-Linking ReagentsLipid BilayersMicellesReceptor, Platelet-Derived Growth Factor betaSuccinimides

Identifiers

PMID22619173
PMCPMC3406703
OpenAlexW2013979901

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.