Evidence map›Paper›PMID 15728719›Full record

ArticleMolecular biology of the cell2005

A mutation in dVps28 reveals a link between a subunit of the endosomal sorting complex required for transport-I complex and the actin cytoskeleton in Drosophila.

Evgueni A Sevrioukov, Nabil Moghrabi, Mary Kuhn, Helmut Krämer

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Genetic and Cell Biology Methods to Study ESCRTs in Drosophila melanogaster.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  8. Membrane Tethering Complexes in the Endosomal System.Frontiers in cell and developmental biology · 2016
    Review
  9. Article
  10. Shaping development with ESCRTs.Nature cell biology · 2011
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Genetic screen identifies serpin5 as a regulator of the toll pathway and CHMP2B toxicity associated with frontotemporal dementia.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  16. Article
  17. Article
  18. Article
  19. ESCRT factors restrict mycobacterial growth.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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

4 authors at 2 institutions in 1 country.

Evgueni A SevrioukovCenter for Basic Neuroscience and Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9111, USA.
Nabil Moghrabi
Mary Kuhn
Helmut Krämer
The University of Texas Southwestern Medical Center · USMassachusetts General Hospital · US

Funding

MOLECULAR ANALYSIS OF THE BOSS TRANSMEMBRANE LIGANDR01EY010199 · NEI · UT SOUTHWESTERN MEDICAL CENTER · PI Helmut J Kramer · 1994 to 2026
$9.7M
Hook proteins in membrane trafficking &neurogenerationR01NS043406 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI KRAMER, HELMUT J · 2002 to 2006
$1.5M
NEI NIH HHS EY-10199NEI NIH HHS R01 EY010199NINDS NIH HHS NS-43406NINDS NIH HHS R01 NS043406
6 · The paper itself

Abstract

Proteins that constitute the endosomal sorting complex required for transport (ESCRT) are necessary for the sorting of proteins into multivesicular bodies (MVBs) and the budding of several enveloped viruses, including HIV-1. The first of these complexes, ESCRT-I, consists of three proteins: Vps28p, Vps37p, and Vps23p or Tsg101 in mammals. Here, we characterize a mutation in the Drosophila homolog of vps28. The dVps28 gene is essential: homozygous mutants die at the transition from the first to second instar. Removal of maternally contributed dVps28 causes early embryonic lethality. In such embryos lacking dVps28, several processes that require the actin cytoskeleton are perturbed, including axial migration of nuclei, formation of transient furrows during cortical divisions in syncytial embryos, and the subsequent cellularization. Defects in actin cytoskeleton organization also become apparent during sperm individualization in dVps28 mutant testis. Because dVps28 mutant cells contained MVBs, these defects are unlikely to be a secondary consequence of disrupted MVB formation and suggest an interaction between the actin cytoskeleton and endosomal membranes in Drosophila embryos earlier than previously appreciated.

Indexed as

ActinsAmino Acid SequenceAnimalsCytoskeletonDrosophilaDrosophila ProteinsEndosomesFemaleGenes, InsectMaleMicroscopy, ElectronMolecular Sequence DataMutationSequence Homology, Amino AcidSpermatogenesisVesicular Transport ProteinsActinsDrosophila ProteinsVesicular Transport Proteins

Identifiers

PMID15728719
PMCPMC1087236
OpenAlexW2168198004

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.