Evidence map›Paper›PMID 23546604›Full record

ArticleEndocrinology2013

Palladin is a regulator of actin filament bundles at the ectoplasmic specialization in adult rat testes.

Xiaojing Qian, Dolores D Mruk, Elissa W P Wong, Pearl P Y Lie, C Yan Cheng

Open access · bronzeAbstract read
In one paragraph

Article in Endocrinology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.2field-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

44 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Spermiation: Insights from Studies on the Adjudin Model.Advances in experimental medicine and biology · 2021
    Review
  8. Microtubule Cytoskeleton and Spermatogenesis-Lesson From Studies of Toxicant Models.Toxicological sciences : an official journal of the Society of Toxicology · 2020
    Review
  9. Article
  10. Cdc42 is involved in NC1 peptide-regulated BTB dynamics through actin and microtubule cytoskeletal reorganization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Drebrin and Spermatogenesis.Advances in experimental medicine and biology · 2017
    Article
  17. Review
  18. Article
  19. Review
  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

5 authors at 2 institutions in 2 countries.

Xiaojing QianMary M. Wohlford Laboratory for Male Contraceptive Research, Center for Biomedical Research, Population Council, 1230 York Ave, New York, New York 10065, USA.
Dolores D Mruk
Elissa W P Wong
Pearl P Y Lie
C Yan Cheng
Population Council · USPeking Union Medical College Hospital · CN

Funding

SPECIALIZED CONTRACEPTIVE DEVELOPMENT RESEARCH CENTERU54HD029990 · NICHD · POPULATION COUNCIL · PI WARE, REGINE SITRUK · 1992 to 2016
$27.7M
The biology of blood-testis barrier dynamicsR01HD056034 · NICHD · POPULATION COUNCIL · PI CHENG, C. YAN · 2009 to 2018
$3.4M
NICHD NIH HHS R01 HD056034NICHD NIH HHS U54 HD029990
6 · The paper itself

Abstract

In rat testes, the ectoplasmic specialization (ES) at the Sertoli-Sertoli and Sertoli-spermatid interface known as the basal ES at the blood-testis barrier and the apical ES in the adluminal compartment, respectively, is a testis-specific adherens junction. The remarkable ultrastructural feature of the ES is the actin filament bundles that sandwiched in between the cisternae of endoplasmic reticulum and apposing plasma membranes. Although these actin filament bundles undergo extensive reorganization to switch between their bundled and debundled state to facilitate blood-testis barrier restructuring and spermatid adhesion/transport, the regulatory molecules underlying these events remain unknown. Herein we report findings of an actin filament cross-linking/bundling protein palladin, which displayed restrictive spatiotemporal expression at the apical and the basal ES during the epithelial cycle. Palladin structurally interacted and colocalized with Eps8 (epidermal growth factor receptor pathway substrate 8, an actin barbed end capping and bundling protein) and Arp3 (actin related protein 3, which together with Arp2 form the Arp2/3 complex to induce branched actin nucleation, converting bundled actin filaments to an unbundled/branched network), illustrating its role in regulating actin filament bundle dynamics at the ES. A knockdown of palladin in Sertoli cells in vitro with an established tight junction (TJ)-permeability barrier was found to disrupt the TJ function, which was associated with a disorganization of actin filaments that affected protein distribution at the TJ. Its knockdown in vivo also perturbed F-actin organization that led to a loss of spermatid polarity and adhesion, causing defects in spermatid transport and spermiation. In summary, palladin is an actin filament regulator at the ES.

Indexed as

Actin CytoskeletonAge FactorsAnimalsBlood-Testis BarrierCell DifferentiationCells, CulturedCytoskeletal ProteinsHydrazinesIndazolesMalePhosphoproteinsRatsRats, Sprague-DawleyRats, TransgenicSertoli CellsTestis1-(2,4-dichlorobenzyl)indazole-3-carbohydrazideCytoskeletal ProteinsHydrazinesIndazolesLOC103693936Phosphoproteins

Identifiers

PMID23546604
PMCPMC3628023
OpenAlexW2107170177

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.