Evidence map›Paper›PMID 10760246›Full record

ArticleThe Plant cell2000

Maize profilin isoforms are functionally distinct.

D R Kovar, B K Drøbak, C J Staiger

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

81 citing papers in PubMed, 191 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article
  11. Review
  12. Article
  13. Mechanism of CAP1-mediated apical actin polymerization in pollen tubes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Review
  15. Article
  16. Simultaneous imaging and functional studies reveal a tight correlation between calcium and actin networks.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Review
  18. Review
  19. Article
  20. Article

21 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

3 authors at 2 institutions in 2 countries.

D R KovarDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
B K Drøbak
C J Staiger
Purdue University West Lafayette · USJohn Innes Centre · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Profilin is an actin monomer binding protein that, depending on the conditions, causes either polymerization or depolymerization of actin filaments. In plants, profilins are encoded by multigene families. In this study, an analysis of native and recombinant proteins from maize demonstrates the existence of two classes of functionally distinct profilin isoforms. Class II profilins, including native endosperm profilin and a new recombinant protein, ZmPRO5, have biochemical properties that differ from those of class I profilins. Class II profilins had higher affinity for poly-l-proline and sequestered more monomeric actin than did class I profilins. Conversely, a class I profilin inhibited hydrolysis of membrane phosphatidylinositol-4,5-bisphosphate by phospholipase C more strongly than did a class II profilin. These biochemical properties correlated with the ability of class II profilins to disrupt actin cytoplasmic architecture in live cells more rapidly than did class I profilins. The actin-sequestering activity of both maize profilin classes was found to be dependent on the concentration of free calcium. We propose a model in which profilin alters cellular concentrations of actin polymers in response to fluctuations in cytosolic calcium concentration. These results provide strong evidence that the maize profilin gene family consists of at least two classes, with distinct biochemical and live-cell properties, implying that the maize profilin isoforms perform distinct functions in the plant.

Indexed as

Contractile ProteinsZea maysActinsAdenosine TriphosphateAmino Acid SequenceCalciumCloning, MolecularCytoplasmHumansHydrolysisMicrofilament ProteinsMolecular Sequence DataPeptidesPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol Diacylglycerol-LyasePlant ProteinsActinsAdenosine TriphosphateCalciumContractile ProteinsMicrofilament ProteinsPeptidesPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol Diacylglycerol-LyasePlant ProteinspolyprolineProfilinsProtein IsoformsRecombinant ProteinsRNA, MessengerType C Phospholipases

Identifiers

PMID10760246
PMCPMC139855
OpenAlexW2130872184

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.