Evidence map›Paper›PMID 15349788›Full record

ArticleChromosoma2004

SUMO modified proteins localize to the XY body of pachytene spermatocytes.

Richard S Rogers, Amy Inselman, Mary Ann Handel, Michael J Matunis

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Chromosoma, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

54 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. SIRT1: A Key Player in Male Reproduction.Life (Basel, Switzerland) · 2022
    Review
  7. Histone Chaperones as Cardinal Players in Development.Frontiers in cell and developmental biology · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
  13. Article
  14. DNA damage response protein TOPBP1 regulates X chromosome silencing in the mammalian germ line.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Cross-talk between sumoylation and phosphorylation in mouse spermatocytes.Biochemical and biophysical research communications · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Wrestling with Chromosomes: The Roles of SUMO During Meiosis.Advances in experimental medicine and biology · 2017
    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

4 authors at 3 institutions in 1 country.

Richard S RogersDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Amy Inselman
Mary Ann Handel
Michael J Matunis
University of Tennessee at Knoxville · USInstitute for Systems Biology · USJohns Hopkins University · US

Funding

Regulation and Function of SUMO Protein Modification -Equipment SupplementR01GM060980 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J. · 2000 to 2023
$7.1M
CELL CYCLE REGULATION DURING SPERMATOGENESISR01HD033816 · NICHD · UNIVERSITY OF TENNESSEE KNOXVILLE · PI HANDEL, MARY ANN · 1996 to 2016
$4.7M
NICHD NIH HHS R01 HD033816NICHD NIH HHS R01 HD33816NIGMS NIH HHS R01 GM060980NIGMS NIH HHS R01 GM60980
6 · The paper itself

Abstract

The XY body is a specialized chromatin territory that forms during meiotic prophase of spermatogenesis and comprises the transcriptionally repressed sex chromosomes. Remodeling of the XY chromatin is brought about by recruitment of specific proteins to the X and Y chromosomes during meiosis, and also by post-translational modifications of histones and other chromatin-associated proteins. Here, we demonstrate that SUMO, a small ubiquitin-related modifier protein that regulates a wide variety of nuclear functions in somatic cells, dramatically localizes to the XY body. SUMO was first detected in the XY body of early pachytene spermatocytes and gradually accumulated, reaching maximal levels there during the mid to late pachytene stages. Several known SUMO substrates, including PML and DAXX, were also found to accumulate in the XY body of mid to late stage pachytene spermatocytes. These same proteins localize to PML nuclear bodies of somatic interphase nuclei. Together, these findings indicate a role for SUMO modification in regulating the structure and function of the XY body and reveal molecular similarities between the XY body and PML nuclear bodies.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsApoptosisCarrier ProteinsCell NucleusCo-Repressor ProteinsIntracellular Signaling Peptides and ProteinsMaleMiceMice, KnockoutMolecular ChaperonesNeoplasm ProteinsNuclear ProteinsPachytene StagePromyelocytic Leukemia ProteinRatsAdaptor Proteins, Signal TransducingCarrier ProteinsCo-Repressor ProteinsDAXX protein, humanIntracellular Signaling Peptides and ProteinsMolecular ChaperonesNeoplasm ProteinsNuclear ProteinsPml protein, mousePromyelocytic Leukemia ProteinSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID15349788
OpenAlexW2094973438

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.