Evidence map›Paper›PMID 9634586›Full record

ArticleThe Plant cell1998

Pollen profilin function depends on interaction with proline-rich motifs.

B C Gibbon, L E Zonia, D R Kovar, P J Hussey, C J Staiger

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in The Plant cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Root hairs.The arabidopsis book · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Panallergens and their impact on the allergic patient.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2010
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. New views on the plant cytoskeleton.Plant physiology · 2004
    Review
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

B C GibbonDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
L E Zonia
D R Kovar
P J Hussey
C J Staiger
Purdue University West Lafayette · USRoyal Holloway University of London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin binding protein profilin has dramatic effects on actin polymerization in vitro and in living cells. Plants have large multigene families encoding profilins, and many cells or tissues can express multiple profilin isoforms. Recently, we characterized several profilin isoforms from maize pollen for their ability to alter cytoarchitecture when microinjected into living plant cells and for their association with poly-L-proline and monomeric actin from maize pollen. In this study, we characterize a new profilin isoform from maize, which has been designated ZmPRO4, that is expressed predominantly in endosperm but is also found at low levels in all tissues examined, including mature and germinated pollen. The affinity of ZmPRO4 for monomeric actin, which was measured by two independent methods, is similar to that of the three profilin isoforms previously identified in pollen. In contrast, the affinity of ZmPRO4 for poly-L-proline is nearly twofold higher than that of native pollen profilin and the other recombinant profilin isoforms. When ZmPRO4 was microinjected into plant cells, the effect on actin-dependent nuclear position was significantly more rapid than that of another pollen profilin isoform, ZmPRO1. A gain-of-function mutant (ZmPRO1-Y6F) was created and found to enhance poly-L-proline binding activity and to disrupt cytoarchitecture as effectively as ZmPRO4. In this study, we demonstrate that profilin isoforms expressed in a single cell can have different effects on actin in living cells and that the poly-L-proline binding function of profilin may have important consequences for the regulation of actin cytoskeletal dynamics in plant cells.

Indexed as

Contractile ProteinsProlineActinsAmino Acid SequenceBinding SitesCell NucleusCloning, MolecularEscherichia coliMicrofilament ProteinsMolecular Sequence DataPeptidesPlant ProteinsPollenPolymerase Chain ReactionProfilinsProtein BindingActinsContractile ProteinsMicrofilament ProteinsPeptidesPlant ProteinspolyprolineProfilinsProlineRecombinant Proteins

Identifiers

PMID9634586
PMCPMC144034
OpenAlexW2157425510

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.