Evidence map›Paper›PMID 10973991›Full record

ArticleThe Journal of cell biology2000

Profilin enhances Cdc42-induced nucleation of actin polymerization.

C Yang, M Huang, J DeBiasio, M Pring, M Joyce, H Miki, T Takenawa, S H Zigmond

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 131 citations in OpenAlex.

  1. Review
  2. Neutrophil attachment via Mac-1 (Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  3. Article
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  14. Review
  15. Article
  16. Cytoskeletal actin networks in motile cells are critically self-organized systems synchronized by mechanical interactions.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle.Journal of cardiovascular pharmacology and therapeutics · 2008
    Review
  19. Article
  20. Review
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

8 authors at 2 institutions in 2 countries.

C YangDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6018, USA.
M Huang
J DeBiasio
M Pring
M Joyce
H Miki
T Takenawa
S H Zigmond
University of Pennsylvania · USTokyo University of Science · JP

Funding

CELL BIOLOGY OF LOCOMOTION AND CHEMOTAXIS OF LEUKOCYTESR37AI019883 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI ZIGMOND, SALLY H · 1994 to 2003
$1.6M
PINOCYTOSIS IN POLYMORPHONUCLEAR LEUKOCYTESR01AI019883 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI ZIGMOND, SALLY H · 1985 to 1992
–
NIAID NIH HHS AI 19883
6 · The paper itself

Abstract

We find that profilin contributes in several ways to Cdc42-induced nucleation of actin filaments in high speed supernatant of lysed neutrophils. Depletion of profilin inhibited Cdc42-induced nucleation; re-addition of profilin restored much of the activity. Mutant profilins with a decreased affinity for either actin or poly-l-proline were less effective at restoring activity. Whereas Cdc42 must activate Wiskott-Aldrich Syndrome protein (WASP) to stimulate nucleation by the Arp2/3 complex, VCA (verpolin homology, cofilin, and acidic domain contained in the COOH-terminal fragment of N-WASP) constitutively activates the Arp2/3 complex. Nucleation by VCA was not inhibited by profilin depletion. With purified N-WASP and Arp2/3 complex, Cdc42-induced nucleation did not require profilin but was enhanced by profilin, wild-type profilin being more effective than mutant profilin with reduced affinity for poly-l-proline. Nucleation by the Arp2/3 complex is a function of the free G-actin concentration. Thus, when profilin addition decreased the free G-actin concentration, it inhibited Cdc42- and VCA-induced nucleation. However, when profilin was added with G-actin in a ratio that maintained the initial free G-actin concentration, it increased the rate of both Cdc42- and VCA-induced nucleation. This enhancement, also seen with purified proteins, was greatest when the free G-actin concentration was low. These data suggest that under conditions present in intact cells, profilin enhances nucleation by activated Arp2/3 complex.

Indexed as

Contractile ProteinsActinsAmino Acid SubstitutionAnimalsBinding Sitescdc42 GTP-Binding ProteinCell LineHumansKineticsMacromolecular SubstancesMicrofilament ProteinsMutagenesis, Site-DirectedNeutrophilsPeptidesProfilinsProteinsActinscdc42 GTP-Binding ProteinContractile ProteinsMacromolecular SubstancesMicrofilament ProteinsPeptidesPFN1 protein, humanpolyprolineProfilinsProteinsRecombinant Fusion ProteinsWAS protein, humanWiskott-Aldrich Syndrome Protein

Identifiers

PMID10973991
PMCPMC2175244
OpenAlexW2122213969

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.