Evidence map›Paper›PMID 9034331›Full record

ArticleThe EMBO journal1997

The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences.

A Lambrechts, J L Verschelde, V Jonckheere, M Goethals, J Vandekerckhove, C Ampe

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Profilin Isoforms in Health and Disease - All the Same but Different.Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article
  10. Emerging Functions of Actins and Actin Binding Proteins in Trypanosomatids.Frontiers in cell and developmental biology · 2020
    Review
  11. Article
  12. Review
  13. Structural basis for mutation-induced destabilization of profilin 1 in ALS.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. The role of actin filament dynamics in the myogenic response of cerebral resistance arteries.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2013
    Review
  17. Article
  18. Article
  19. Fine-tuning of neuronal architecture requires two profilin isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. 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

6 authors at 1 institution in 1 country.

A LambrechtsDepartment of Biochemistry, Faculty of Medicine, Universiteit Gent, Belgium.
J L Verschelde
V Jonckheere
M Goethals
J Vandekerckhove
C Ampe
Ghent University · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a study on the binding properties of the bovine profilin isoforms to both phosphatidylinositol 4,5-bisphosphate (PIP2) and proline-rich peptides derived from vasodilator-stimulated phosphoprotein (VASP) and cyclase-associated protein (CAP). Using microfiltration, we show that compared with profilin II, profilin I has a higher affinity for PIP2. On the other hand, fluorescence spectroscopy reveals that proline-rich peptides bind better to profilin II. At micromolar concentrations, profilin II dimerizes upon binding to proline-rich peptides. Circular dichroism measurements of profilin II reveal a significant conformational change in this protein upon binding of the peptide. We show further that PIP2 effectively competes for binding of profilin I to poly-L-proline, since this isoform, but not profilin II, can be eluted from a poly-L-proline column with PIP2. Using affinity chromatography on either profilin isoform, we identified profilin II as the preferred ligand for VASP in bovine brain extracts. The complementary affinities of the profilin isoforms for PIP2 and the proline-rich peptides offer the cell an opportunity to direct actin assembly at different subcellular localizations through the same or different signal transduction pathways.

Indexed as

Cell Cycle ProteinsContractile ProteinsCytoskeletal ProteinsDrosophila ProteinsAmino Acid SequenceAnimalsBinding, CompetitiveBinding SitesBlotting, WesternBrainCattleCell Adhesion MoleculesCircular DichroismDimerizationElectrophoresis, Polyacrylamide GelFungal ProteinsCapt protein, DrosophilaCell Adhesion MoleculesCell Cycle ProteinsContractile ProteinsCytoskeletal ProteinsDrosophila ProteinsFungal ProteinsMicrofilament ProteinsPeptide FragmentsPeptidesPhosphatidylinositol 4,5-DiphosphatePhosphoproteinspolyprolineProfilinsVasodilator-Stimulated Phosphoprotein

Identifiers

PMID9034331
PMCPMC1169652
OpenAlexW2022122132

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.