Evidence map›Paper›PMID 23077236›Full record

ArticleHuman reproduction (Oxford, England)2013

Localization and identification of sumoylated proteins in human sperm: excessive sumoylation is a marker of defective spermatozoa.

Margarita Vigodner, Vibha Shrivastava, Leah Elisheva Gutstein, Jordana Schneider, Edward Nieves, Marc Goldstein, Miriam Feliciano, Myrasol Callaway

Open access · bronzeAbstract read
In one paragraph

Article in Human reproduction (Oxford, England), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Sumoylation and its regulation in testicular Sertoli cells.Biochemical and biophysical research communications · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Regulation of germ cell function by SUMOylation.Cell and tissue research · 2016
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 3 institutions in 1 country.

Margarita VigodnerDepartment of Biology, Stern College, Yeshiva University, 245 Lexington Avenue, New York, NY 10016, USA. vigodner@yu.edu
Vibha Shrivastava
Leah Elisheva Gutstein
Jordana Schneider
Edward Nieves
Marc Goldstein
Miriam Feliciano
Myrasol Callaway
Albert Einstein College of Medicine · USYeshiva University · USCornell University · US

Funding

LTQ Orbitrap Velos Mass Spectrometer SystemS10RR029398 · NCRR · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI ANGELETTI, RUTH HOGUE · 2010 to 2010
$963k
Regulation of spermatogenesis by sumoylationR15HD067944 · NICHD · YESHIVA UNIVERSITY · PI VIGODNER, MARGARITA · 2011 to 2014
$600k
MASS SPECTROMETER SYSTEM: OBESITYS10RR019352 · NCRR · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI ANGELETTI, RUTH HOGUE · 2004 to 2004
$379k
NCRR NIH HHS 1S10RR019352NCRR NIH HHS 1S10RR029398NICHD NIH HHS R15 HD067944-01A1
6 · The paper itself

Abstract

backgroundSumoylation is a type of post-translational modification that is implicated in the regulation of numerous cellular events. However, its role in the function of human sperm has not yet been characterized. METHODS AND

resultsIn this study, both immunofluorescence and electron microscopy revealed that small ubiquitin-like modifiers (SUMO) SUMO1 and SUMO2/3 were highly enriched in the neck area of human sperm that is associated with the redundant nuclear envelope and were also detectable in the flagella and some head regions. Similar localization patterns of SUMO were also observed in mouse and fly sperm. Nonmotile, two-tailed, curled tailed, misshapen, microcephalic (small head) and aciphalic (no head) sperm exhibited abnormally high levels of sumoylation in their neck and tail regions relative to normal sperm. Numerous sumoylated proteins, ranging from 20 to 260 kDa, were detected via western blotting and identified by mass spectrometry, and 55 SUMO targets that were present specifically in human sperm, and not in the control fraction, corresponded to flagella proteins, proteins involved in the maturation and differentiation of sperm, heat shock proteins and important glycolytic and mitochondrial enzymes. The targets that were identified included proteins with specific functions in germ cells and sperm, such as heat shock-related 70-kDa protein 2, outer dense fiber protein 3, A-kinase anchor proteins 3 and 4, L-lactate dehydrogenase C, sperm protein associated with the nucleus on the X chromosome B/F, valosin-containing protein, seminogelins, histone H4 and ubiquitin. Coimmunoprecipitation experiments confirmed the sumoylation of semenogelin and indicated that some sperm proteins are modified by sumoylation and ubiquitination simultaneously.

conclusionsNumerous proteins are modified by sumoylation in human sperm; excessive sumoylation is a marker of defective spermatozoa.

Indexed as

AnimalsBiomarkersCell ShapeDipteraEpididymisHumansInfertility, MaleInsect ProteinsMaleMiceMolecular WeightNuclear EnvelopePeptide FragmentsProteinsProtein TransportSmall Ubiquitin-Related Modifier ProteinsBiomarkersInsect ProteinsPeptide FragmentsProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, humanSUMO3 protein, humanUbiquitins

Identifiers

PMID23077236
PMCPMC3522414
OpenAlexW2099023028

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.