Evidence map›Paper›PMID 28500503›Full record

ArticleHistochemistry and cell biology2017

Expression and localization of myosin VI in developing mouse spermatids.

Przemysław Zakrzewski, Robert Lenartowski, Maria Jolanta Rędowicz, Kathryn G Miller, Marta Lenartowska

Open access · hybridAbstract read
In one paragraph

Article in Histochemistry and cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.2field-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

13 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. In focus in HCB.Histochemistry and cell biology · 2019
    Article
  13. 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 3 institutions in 2 countries.

Przemysław ZakrzewskiLaboratory of Developmental Biology, Faculty of Biology and Environmental Protection, Nicolaus Copernicus University in Toruń, Toruń, Poland. przezak@doktorant.umk.pl.ORCID http://orcid.org/0000-0003-0035-5509
Robert LenartowskiLaboratory of Isotope and Instrumental Analysis, Faculty of Biology and Environmental Protection, Nicolaus Copernicus University in Toruń, Toruń, Poland.
Maria Jolanta RędowiczLaboratory of Molecular Basis of Cell Motility, Department of Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.
Kathryn G MillerDepartment of Biology, Washington University in St. Louis, St. Louis, MO, USA.
Marta LenartowskaLaboratory of Developmental Biology, Faculty of Biology and Environmental Protection, Nicolaus Copernicus University in Toruń, Toruń, Poland.
Nicolaus Copernicus University · PLInstytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLWashington University in St. Louis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin VI (MVI) is a versatile actin-based motor protein that has been implicated in a variety of different cellular processes, including endo- and exocytic vesicle trafficking, Golgi morphology, and actin structure stabilization. A role for MVI in crucial actin-based processes involved in sperm maturation was demonstrated in Drosophila. Because of the prominence and importance of actin structures in mammalian spermiogenesis, we investigated whether MVI was associated with actin-mediated maturation events in mammals. Both immunofluorescence and ultrastructural analyses using immunogold labeling showed that MVI was strongly linked with key structures involved in sperm development and maturation. During the early stage of spermiogenesis, MVI is associated with the Golgi and with coated and uncoated vesicles, which fuse to form the acrosome. Later, as the acrosome spreads to form a cap covering the sperm nucleus, MVI is localized to the acroplaxome, an actin-rich structure that anchors the acrosome to the nucleus. Finally, during the elongation/maturation phase, MVI is associated with the actin-rich structures involved in nuclear shaping: the acroplaxome, manchette, and Sertoli cell actin hoops. Since this is the first report of MVI expression and localization during mouse spermiogenesis and MVI partners in developing sperm have not yet been identified, we discuss some probable roles for MVI in this process. During early stages, MVI is hypothesized to play a role in Golgi morphology and function as well as in actin dynamics regulation important for attachment of developing acrosome to the nuclear envelope. Next, the protein might also play anchoring roles to help generate forces needed for spermatid head elongation. Moreover, association of MVI with actin that accumulates in the Sertoli cell ectoplasmic specialization and other actin structures in surrounding cells suggests additional MVI functions in spermatid movement across the seminiferous epithelium and in sperm release.

Indexed as

Alternative SplicingAnimalsGenetic VariationImmunohistochemistryMaleMiceMyosin Heavy ChainsSpermatidsMyosin Heavy Chainsmyosin VIActinImmunocytochemistryMyosin VI splice variantsSpermiogenesisUltrastructure

Identifiers

PMID28500503
PMCPMC5602056
OpenAlexW2612046321

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.