Evidence map›Paper›PMID 10588662›Full record

ArticleMolecular biology of the cell1999

Class VI unconventional myosin is required for spermatogenesis in Drosophila.

J L Hicks, W M Deng, A D Rogat, K G Miller, M Bownes

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Myosin VI is expressed in developing ovarian follicles inFrontiers in cell and developmental biology · 2025
    Article
  3. Article
  4. Article
  5. Unconventional translation initiation factor EIF2A is required for Drosophila spermatogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2022
    Article
  6. Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021
    Review
  7. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Structure of androcam supports specialized interactions with myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

5 authors at 2 institutions in 2 countries.

J L HicksDepartment of Biology, Washington University, St. Louis, Missouri 63130, USA.
W M Deng
A D Rogat
K G Miller
M Bownes
Washington University in St. Louis · USUniversity of Edinburgh · GB

Funding

FUNCTION OF 95F UNCONVENTIONAL MYOSIN IN DROSOPHILAR01GM043607 · NIGMS · WASHINGTON UNIVERSITY · PI MILLER, KATHRYN G · 1995 to 1997
–
ACTIN-BINDING PROTEINS AND DROSOPHILA EMBRYOSR29GM043607 · NIGMS · WASHINGTON UNIVERSITY · PI MILLER, KATHRYN G · 1990 to 1994
–
NIGMS NIH HHS GM-43607Wellcome Trust
6 · The paper itself

Abstract

We have identified partial loss of function mutations in class VI unconventional myosin, 95F myosin, which results in male sterility. During spermatogenesis the germ line precursor cells undergo mitosis and meiosis to form a bundle of 64 spermatids. The spermatids remain interconnected by cytoplasmic bridges until individualization. The process of individualization involves the formation of a complex of cytoskeletal proteins and membrane, the individualization complex (IC), around the spermatid nuclei. This complex traverses the length of each spermatid resolving the shared membrane into a single membrane enclosing each spermatid. We have determined that 95F myosin is a component of the IC whose function is essential for individualization. In wild-type testes, 95F myosin localizes to the leading edge of the IC. Two independent mutations in 95F myosin reduce the amount of 95F myosin in only a subset of tissues, including the testes. This reduction of 95F myosin causes male sterility as a result of defects in spermatid individualization. Germ line transformation with the 95F myosin heavy chain cDNA rescues the male sterility phenotype. IC movement is aberrant in these 95F myosin mutants, indicating a critical role for 95F myosin in IC movement. This report is the first identification of a component of the IC other than actin. We propose that 95F myosin is a motor that participates in membrane reorganization during individualization.

Indexed as

ActinsAnimalsDNA Transposable ElementsDrosophilaFluorescent Antibody TechniqueInfertility, MaleMaleMutagenesis, InsertionalMutationMyosin Heavy ChainsPhenotypeReverse Transcriptase Polymerase Chain ReactionSpermatogenesisTestisActinsDNA Transposable ElementsMyosin Heavy Chainsmyosin VI

Identifiers

PMID10588662
PMCPMC25762
OpenAlexW2102395239

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.