Evidence map›Paper›PMID 8416982›Full record

ArticleThe Journal of cell biology1993

Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein.

K R Fath, D R Burgess

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

51 citing papers in PubMed, 189 citations in OpenAlex.

  1. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  2. Article
  3. Article
  4. Actin acting at the Golgi.Histochemistry and cell biology · 2013
    Review
  5. Article
  6. Article
  7. Article
  8. Review
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  10. Article
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  15. Review
  16. Article
  17. The golgi-associated COPI-coated buds and vesicles contain beta/gamma -actin.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  18. VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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

2 authors at 1 institution in 1 country.

K R FathDepartment of Biological Sciences, University of Pittsburgh, Pennsylvania 15260.
D R Burgess
University of Pittsburgh · US

Funding

CONTROL OF BRUSH BORDER MOTILITY AND MICROVILLUS GROWTHR01DK031643 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BURGESS, DAVID · 1986 to 1998
–
NIDDK NIH HHS DK 31643
6 · The paper itself

Abstract

In the intestinal brush border, the mechanoenzyme myosin-I links the microvillus core actin filaments with the plasma membrane. Previous immunolocalization shows that myosin-I is associated with vesicles in mature enterocytes (Drenckhahn, D., and R. Dermietzel. 1988. J. Cell Biol. 107:1037-1048) suggesting a potential role mediating vesicle motility. We now report that myosin-I is associated with Golgi-derived vesicles isolated from cells that are rapidly assembling brush borders in intestinal crypts. Crypt cells were isolated in hyperosmotic buffer, homogenized, and fractionated using differential- and equilibrium-density centrifugation. Fractions containing 50-100-nm vesicles, a similar size to those observed in situ, were identified by EM and were shown to contain myosin-I as demonstrated by immunoblotting and immunolabel negative staining. Galactosyltransferase, a marker enzyme for trans-Golgi membranes was present in these fractions, as was alkaline phosphatase, which is an apical membrane targeted enzyme. Galactosyltransferase was also present in vesicles immuno-purified with antibodies to myosin-I. Villin, a marker for potential contamination from fragmented microvilli, was absent. Myosin-I was found to reside on the vesicle "outer" or cytoplasmic surface for it was accessible to exogenous proteases and intact vesicles could be immunolabeled with myosin-I antibodies in solution. The bound myosin-I could be extracted from the vesicles using NaCl, KI and Na2CO3, suggesting that it is a vesicle peripheral membrane protein. These vesicles were shown to bundle actin filaments in an ATP-dependent manner. These results are consistent with a role for myosin-I as an apically targeted motor for vesicle translocation in epithelial cells.

Indexed as

Cell PolarityActinsAlkaline PhosphataseAnimalsBiological TransportCell CompartmentationChickensEpithelial CellsEpitheliumGalactosyltransferasesGolgi ApparatusIntestinal MucosaIntracellular MembranesMembrane ProteinsMicrovilliMyosinsActinsAlkaline PhosphataseGalactosyltransferasesMembrane ProteinsMyosins

Identifiers

PMID8416982
PMCPMC2119486
OpenAlexW2164516476

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.