Evidence map›Paper›PMID 19029335›Full record

ArticleThe Journal of cell biology2008

Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding.

Christian Frantz, Gabriela Barreiro, Laura Dominguez, Xiaoming Chen, Robert Eddy, John Condeelis, Mark J S Kelly, Matthew P Jacobson, Diane L Barber

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 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing 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

112 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Evolution of pH-sensitive transcription termination inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. pH-regulated single cell migration.Pflugers Archiv : European journal of physiology · 2024
    Review
  10. Article
  11. MARCKS and PI(4,5)PMolecular biology of the cell · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Review

52 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

9 authors.

Christian FrantzDepartment of Cell and Tissue Biology, University of California, San Francisco, CA 94143, USA.
Gabriela Barreiro
Laura Dominguez
Xiaoming Chen
Robert Eddy
John Condeelis
Mark J S Kelly
Matthew P Jacobson
Diane L Barber

Funding

Actions of the Sodium-Hydrogen Exchanger Subtype, NHE1R01GM058642 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BARBER, DIANE L · 1999 to 2012
$3.4M
SIGNAL TRANSDUCTION AND ACTIN DURING AMOEBOID CHEMOTAXISR01GM038511 · NIGMS · YESHIVA UNIVERSITY · PI CONDEELIS, JOHN S · 1988 to 2008
$2.8M
PROGRAM IN CRANIOFACIAL &SKELETAL BIOC06RR016490 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BERTOLAMI, CHARLES N · 2001 to 2001
$2.0M
NCRR NIH HHS C06 RR016490NIGMS NIH HHS GM38511NIGMS NIH HHS GM58642NIGMS NIH HHS R01 GM038511NIGMS NIH HHS R01 GM058642
6 · The paper itself

Abstract

Newly generated actin free barbed ends at the front of motile cells provide sites for actin filament assembly driving membrane protrusion. Growth factors induce a rapid biphasic increase in actin free barbed ends, and we found both phases absent in fibroblasts lacking H(+) efflux by the Na-H exchanger NHE1. The first phase is restored by expression of mutant cofilin-H133A but not unphosphorylated cofilin-S3A. Constant pH molecular dynamics simulations and nuclear magnetic resonance (NMR) reveal pH-sensitive structural changes in the cofilin C-terminal filamentous actin binding site dependent on His133. However, cofilin-H133A retains pH-sensitive changes in NMR spectra and severing activity in vitro, which suggests that it has a more complex behavior in cells. Cofilin activity is inhibited by phosphoinositide binding, and we found that phosphoinositide binding is pH-dependent for wild-type cofilin, with decreased binding at a higher pH. In contrast, phosphoinositide binding by cofilin-H133A is attenuated and pH insensitive. These data suggest a molecular mechanism whereby cofilin acts as a pH sensor to mediate a pH-dependent actin filament dynamics.

Indexed as

Cell MovementActin CytoskeletonActin Depolymerizing FactorsActinsAnimalsBinding SitesCell LineFibroblastsHumansHydrogen-Ion ConcentrationMicrofilament ProteinsModels, MolecularMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositolsPhosphorylationActin Depolymerizing FactorsActinsactophorin protein, AcanthamoebaMicrofilament ProteinsPhosphatidylinositolsPlatelet-Derived Growth FactorProtozoan ProteinsSodium-Hydrogen Exchangers

Identifiers

PMID19029335
PMCPMC2592832

What OpenQuestion holds

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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.