Evidence map›Paper›PMID 19419568›Full record

ArticleBMC cell biology2009

Testis-expressed profilins 3 and 4 show distinct functional characteristics and localize in the acroplaxome-manchette complex in spermatids.

Martina Behnen, Kai Murk, Petri Kursula, Heike Cappallo-Obermann, Martin Rothkegel, Abraham L Kierszenbaum, Christiane Kirchhoff

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Profilin Isoforms in Health and Disease - All the Same but Different.Frontiers in cell and developmental biology · 2021
    Review
  11. Article
  12. Article
  13. Sperm Differentiation: The Role of Trafficking of Proteins.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article
  16. Article
  17. Article
  18. Recombinant production, crystallization and preliminary structural characterization of Schistosoma japonicum profilin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  19. Article
  20. mDia1-3 in mammalian filopodia.Communicative & integrative biology · 2012
    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

7 authors at 4 institutions in 3 countries.

Martina BehnenDepartment of Andrology, University Hospital Hamburg-Eppendorf, Germany. martinabehnen@gmx.de
Kai Murk
Petri Kursula
Heike Cappallo-Obermann
Martin Rothkegel
Abraham L Kierszenbaum
Christiane Kirchhoff
Universität Hamburg · DENew York Medical College · USUniversity Medical Center Hamburg-Eppendorf · DEUniversity of Oulu · FI

Funding

MICROTUBULE/KERATIN INTERACTIONS DURING SPERMATOGENESISR01HD037282 · NICHD · CITY COLLEGE OF NEW YORK · PI KIERSZENBAUM, ABRAHAM L · 1999 to 2002
$692k
NICHD NIH HHS HD 37282NICHD NIH HHS R01 HD037282
6 · The paper itself

Abstract

backgroundMultiple profilin isoforms exist in mammals; at least four are expressed in the mammalian testis. The testis-specific isoforms profilin-3 (PFN3) and profilin-4 (PFN4) may have specialized roles in spermatogenic cells which are distinct from known functions fulfilled by the "somatic" profilins, profilin-1 (PFN1) and profilin-2 (PFN2).

resultsLigand interactions and spatial distributions of PFN3 and PFN4 were compared by biochemical, molecular and immunological methods; PFN1 and PFN2 were employed as controls. beta-actin, phosphoinositides, poly-L-proline and mDia3, but not VASP, were confirmed as in vitro interaction partners of PFN3. In parallel experiments, PFN4 bound to selected phosphoinositides but not to poly-L-proline, proline-rich proteins, or actin. Immunofluorescence microscopy of PFN3 and PFN4 revealed distinct subcellular locations in differentiating spermatids. Both were associated first with the acroplaxome and later with the transient manchette. Predicted 3D structures indicated that PFN3 has the actin-binding site conserved, but retains only approximately half of the common poly-L-proline binding site. PFN4, in comparison, has lost both, polyproline and actin binding sites completely, which is well in line with the experimental data.

conclusionThe testis-specific isoform PFN3 showed major hallmarks of the well characterized "somatic" profilin isoforms, albeit with distinct binding affinities. PFN4, on the other hand, did not interact with actin or polyproline in vitro. Rather, it seemed to be specialized for phospholipid binding, possibly providing cellular functions which are distinct from actin dynamics regulation.

Indexed as

ActinsAnimalsBinding SitesComputer SimulationHumansKineticsMalePeptidesPhospholipidsProfilinsProtein Structure, TertiaryRatsSpermatidsSpermatogenesisTestisActinsPeptidesPhospholipidspolyprolineProfilins

Identifiers

PMID19419568
PMCPMC2694148
OpenAlexW2045322483

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.