Evidence map›Paper›PMID 19591839›Full record

ArticleJournal of molecular biology2009

Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1.

Jianquan Li, David J E Callaway, Zimei Bu

Abstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. The Intricacies of Renal Phosphate Reabsorption-An Overview.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. A sequence upstream of canonical PDZ-binding motif within CFTR COOH-terminus enhances NHERF1 interaction.American journal of physiology. Lung cellular and molecular physiology · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Kinetic response of a photoperturbed allosteric protein.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. Nanoscale protein dynamics: a new frontier for neutron spin echo spectroscopy.The European physical journal. E, Soft matter · 2013
    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

3 authors at 2 institutions in 1 country.

Jianquan LiFox Chase Cancer Center, Philadelphia, PA 19111, USA.
David J E Callaway
Zimei Bu
Fox Chase Cancer Center · USNew York University · US

Funding

Struture snd Dynamic Determinants of Ion Channel Assembly by Adapter ProteinsR01HL086496 · NHLBI · RESEARCH INST OF FOX CHASE CAN CTR · PI BU, ZIMEI · 2007 to 2011
$2.1M
NHLBI NIH HHS R01 HL086496
6 · The paper itself

Abstract

Scaffolding proteins are molecular switches that control diverse signaling events. The scaffolding protein Na(+)/H(+) exchanger regulatory factor 1 (NHERF1) assembles macromolecular signaling complexes and regulates the macromolecular assembly, localization, and intracellular trafficking of a number of membrane ion transport proteins, receptors, and adhesion/antiadhesion proteins. NHERF1 begins with two modular protein-protein interaction domains-PDZ1 and PDZ2-and ends with a C-terminal (CT) domain. This CT domain binds to ezrin, which, in turn, interacts with cytosekeletal actin. Remarkably, ezrin binding to NHERF1 increases the binding capabilities of both PDZ domains. Here, we use deuterium labeling and contrast variation neutron-scattering experiments to determine the conformational changes in NHERF1 when it forms a complex with ezrin. Upon binding to ezrin, NHERF1 undergoes significant conformational changes in the region linking PDZ2 and its CT ezrin-binding domain, as well as in the region linking PDZ1 and PDZ2, involving very long range interactions over 120 A. The results provide a structural explanation, at mesoscopic scales, of the allosteric control of NHERF1 by ezrin as it assembles protein complexes. Because of the essential roles of NHERF1 and ezrin in intracellular trafficking in epithelial cells, we hypothesize that this long-range allosteric regulation of NHERF1 by ezrin enables the membrane-cytoskeleton to assemble protein complexes that control cross-talk and regulate the strength and duration of signaling.

Indexed as

Allosteric RegulationCytoskeletal ProteinsDeuteriumEzrinHumansMass SpectrometryModels, BiologicalModels, MolecularPhosphoproteinsProtein BindingProtein ConformationProtein Structure, TertiaryScattering, Small AngleSodium-Hydrogen ExchangersStaining and LabelingCytoskeletal ProteinsDeuteriumEzrinPhosphoproteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

PMID19591839
PMCPMC2756645
OpenAlexW1982412212

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.