Evidence map›Paper›PMID 20711465›Full record

ArticlePloS one2010

Mammalian sperm head formation involves different polarization of two novel LINC complexes.

Eva Göb, Johannes Schmitt, Ricardo Benavente, Manfred Alsheimer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing 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

87 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. SUN5 forms a regular protein lattice reinforcing the sperm head-tail junction.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  16. Development of the Connecting Piece in ODF1-Deficient Mouse Spermatids.International journal of molecular sciences · 2022
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27 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Eva GöbDepartment of Cell and Developmental Biology, Biocenter, University of Würzburg, Würzburg, Germany.
Johannes Schmitt
Ricardo Benavente
Manfred Alsheimer
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundLINC complexes are nuclear envelope bridging protein structures formed by interaction of SUN and KASH proteins. They physically connect the nucleus with the peripheral cytoskeleton and are critically involved in a variety of dynamic processes, such as nuclear anchorage, movement and positioning and meiotic chromosome dynamics. Moreover, they are shown to be essential for maintaining nuclear shape.

findingsBased on detailed expression analysis and biochemical approaches, we show here that during mouse sperm development, a terminal cell differentiation process characterized by profound morphogenic restructuring, two novel distinctive LINC complexes are established. They consist either of spermiogenesis-specific Sun3 and Nesprin1 or Sun1eta, a novel non-nuclear Sun1 isoform, and Nesprin3. We could find that these two LINC complexes specifically polarize to opposite spermatid poles likely linking to sperm-specific cytoskeletal structures. Although, as shown in co-transfection/immunoprecipitation experiments, SUN proteins appear to arbitrarily interact with various KASH partners, our study demonstrates that they actually are able to confine their binding to form distinct LINC complexes.

conclusionsFormation of the mammalian sperm head involves assembly and different polarization of two novel spermiogenesis-specific LINC complexes. Together, our findings suggest that theses LINC complexes connect the differentiating spermatid nucleus to surrounding cytoskeletal structures to enable its well-directed shaping and elongation, which in turn is a critical parameter for male fertility.

Indexed as

Amino Acid SequenceAnimalsCytoskeletal ProteinsCytoskeletonGene Expression RegulationHumansMaleMeiosisMembrane ProteinsMiceMolecular Sequence DataNerve Tissue ProteinsNuclear EnvelopeNuclear ProteinsOrgan SpecificityProtein IsoformsCytoskeletal ProteinsMembrane ProteinsNerve Tissue Proteinsnesprin-3 protein, mouseNuclear ProteinsProtein IsoformsSyne1 protein, mouse

Identifiers

PMID20711465
PMCPMC2919408
OpenAlexW2171432112

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LicenceCC BY
Read underepoch 390

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.