Evidence map›Paper›PMID 31467409›Full record

ArticleScientific reports2019

Compartmentalization of the proteasome-interacting proteins during sperm capacitation.

Michal Zigo, Pavla Manaskova-Postlerova, Vera Jonakova, Karl Kerns, Peter Sutovsky

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.6field-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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Techniques to Determine Mammalian Sperm Capacitation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Article
  6. Proteostasis as a Sentry for Sperm Quality and Male Fertility.Advances in experimental medicine and biology · 2025
    Review
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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 4 institutions in 2 countries.

Michal ZigoDivision of Animal Sciences, University of Missouri, Columbia, MO, 65211, USA. michal_zigo_2000@yahoo.com.ORCID http://orcid.org/0000-0002-2964-5940
Pavla Manaskova-PostlerovaLaboratory of Reproductive Biology, Institute of Biotechnology of the Czech Academy of Sciences, Vestec, 25250, Czech Republic.
Vera JonakovaLaboratory of Reproductive Biology, Institute of Biotechnology of the Czech Academy of Sciences, Vestec, 25250, Czech Republic.
Karl KernsDivision of Animal Sciences, University of Missouri, Columbia, MO, 65211, USA.ORCID http://orcid.org/0000-0001-7425-0131
Peter SutovskyDivision of Animal Sciences, University of Missouri, Columbia, MO, 65211, USA.
Czech Academy of Sciences, Institute of Biotechnology · CZCzech University of Life Sciences Prague · CZUniversity of Missouri · USUniversity of Missouri Health System · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is a stable, reversible posttranslational modification of target proteins by covalent ligation of the small chaperone protein ubiquitin. Most commonly ubiquitination targets proteins for degradation/recycling by the 26S proteasome in a well-characterized enzymatic cascade. Studies using human and non-human mammalian spermatozoa revealed the role of the ubiquitin-proteasome system (UPS) in the regulation of fertilization, including sperm-zona pellucida (ZP) interactions as well as the early events of sperm capacitation, the remodeling of the sperm plasma membrane and acrosome, and for the acquisition of sperm fertilizing ability. The present study investigated the activity of UPS during in vitro capacitation of fresh boar spermatozoa in relation to changes in sperm proteome. Parallel and sequential treatments of ejaculated and capacitated spermatozoa under proteasome permissive/inhibiting conditions were used to isolate putative sperm proteasome-associated sperm proteins in a compartment-specific manner. A differential proteomic approach employing 1D PAGE revealed differences in accumulated proteins at the molecular weights of 60, 58, 49, and 35 kDa, and MS analysis revealed the accumulation of proteins previously reported as proteasome co-purifying proteins, as well as some novel proteins. Among others, P47/lactadherin, ACRBP, ADAM5, and SPINK2 (alias SAAI) were processed by the proteasome in a capacitation dependent manner. Furthermore, the capacitation-induced reorganization of the outer acrosomal membrane was slowed down in the presence of proteasomal inhibitors. These novel results support the proposed role of UPS in sperm capacitation and open several new lines of inquiry into sperm capacitation mechanism.

Indexed as

Sperm CapacitationAnimalsCell MembraneMaleProteasome Endopeptidase ComplexProteomicsSpermatozoaSwineATP dependent 26S proteaseProteasome Endopeptidase Complex

Identifiers

PMID31467409
PMCPMC6715765
OpenAlexW2970066159

What OpenQuestion holds

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Registered trials

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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.