Evidence map›Paper›PMID 1330091›Full record

ArticleMolecular biology of the cell1992

The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells.

P J Goldschmidt-Clermont, M I Furman, D Wachsstock, D Safer, V T Nachmias, T D Pollard

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

98 citing papers in PubMed, 295 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Wound Healing from an Actin Cytoskeletal Perspective.Cold Spring Harbor perspectives in biology · 2022
    Review
  8. International journal of molecular sciences · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Susceptibility of cytoskeletal-associated proteins for tumor progression.Cellular and molecular life sciences : CMLS · 2021
    Review
  14. Article
  15. Article
  16. Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020
    Review
  17. Review
  18. Review
  19. Review
  20. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article

38 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

6 authors at 1 institution in 1 country.

P J Goldschmidt-ClermontDepartment of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
M I Furman
D Wachsstock
D Safer
V T Nachmias
T D Pollard
Johns Hopkins University · US

Funding

MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
5KDA PEPTIDE AND ITS INTERACTION WITH ACTINR01AR040840 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI NACHMIAS, VIVIANNE T. · 1991 to 1997
–
NIAMS NIH HHS AR-40840NIGMS NIH HHS GM-26338
6 · The paper itself

Abstract

We present evidence for a new mechanism by which two major actin monomer binding proteins, thymosin beta 4 and profilin, may control the rate and the extent of actin polymerization in cells. Both proteins bind actin monomers transiently with a stoichiometry of 1:1. When bound to actin, thymosin beta 4 strongly inhibits the exchange of the nucleotide bound to actin by blocking its dissociation, while profilin catalytically promotes nucleotide exchange. Because both proteins exchange rapidly between actin molecules, low concentrations of profilin can overcome the inhibitory effects of high concentrations of thymosin beta 4 on the nucleotide exchange. These reactions may allow variations in profilin concentration (which may be regulated by membrane polyphosphoinositide metabolism) to control the ratio of ATP-actin to ADP-actin. Because ATP-actin subunits polymerize more readily than ADP-actin subunits, this ratio may play a key regulatory role in the assembly of cellular actin structures, particularly under circumstances of rapid filament turnover.

Indexed as

Contractile ProteinsActinsAdenosineAdenosine DiphosphateAdenosine TriphosphateBinding, CompetitiveBlood PlateletsHumansMicrofilament ProteinsPhosphatidylinositolsProfilinsThymosinThymosin beta(4)ActinsAdenosineAdenosine DiphosphateAdenosine TriphosphateContractile ProteinsMicrofilament ProteinsPFN1 protein, humanPhosphatidylinositolsProfilinsThymosinThymosin beta(4)

Identifiers

PMID1330091
PMCPMC275662
OpenAlexW2023410605

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.