Evidence map›Paper›PMID 20195380›Full record

ArticlePloS one2010

Molecular model of the microvillar cytoskeleton and organization of the brush border.

Jeffrey W Brown, C James McKnight

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.3field-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

35 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Contribution of TRPC3-mediated CaPflugers Archiv : European journal of physiology · 2023
    Article
  5. Article
  6. Review
  7. Manipulation of microvillar proteins duringFrontiers in cellular and infection microbiology · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Actin Cytoskeleton and Actin-Based Motility.Cold Spring Harbor perspectives in biology · 2018
    Review
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Jeffrey W BrownDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, United States of America.
C James McKnight
Boston University · US

Funding

Localizing and Modeling Headpiece Domains on F-ActinR01GM062886 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI MCKNIGHT, CHRISTOPHER JAMES · 2002 to 2006
$1.2M
NIGMS NIH HHS GM62886NIGMS NIH HHS R01 GM062886
6 · The paper itself

Abstract

backgroundBrush border microvilli are approximately 1-microm long finger-like projections emanating from the apical surfaces of certain, specialized absorptive epithelial cells. A highly symmetric hexagonal array of thousands of these uniformly sized structures form the brush border, which in addition to aiding in nutrient absorption also defends the large surface area against pathogens. Here, we present a molecular model of the protein cytoskeleton responsible for this dramatic cellular morphology. METHODOLOGY/PRINCIPAL

findingsThe model is constructed from published crystallographic and microscopic structures reported by several groups over the last 30+ years. Our efforts resulted in a single, unique, self-consistent arrangement of actin, fimbrin, villin, brush border myosin (Myo1A), calmodulin, and brush border spectrin. The central actin core bundle that supports the microvillus is nearly saturated with fimbrin and villin cross-linkers and has a density similar to that found in protein crystals. The proposed model accounts for all major proteinaceous components, reproduces the experimentally determined stoichiometry, and is consistent with the size and morphology of the biological brush border membrane. CONCLUSIONS/SIGNIFICANCE: The model presented here will serve as a structural framework to explain many of the dynamic cellular processes occurring over several time scales, such as protein diffusion, association, and turnover, lipid raft sorting, membrane deformation, cytoskeletal-membrane interactions, and even effacement of the brush border by invading pathogens. In addition, this model provides a structural basis for evaluating the equilibrium processes that result in the uniform size and structure of the highly dynamic microvilli.

Indexed as

Models, MolecularActin CytoskeletonActinsAnimalsCalmodulinCrystallizationCytoskeletonMembrane GlycoproteinsMicrofilament ProteinsMicrovilliMyosinsProtein ConformationSpectrinActinsCalmodulinMembrane GlycoproteinsMicrofilament ProteinsMyosinsplastinSpectrinvillin

Identifiers

PMID20195380
PMCPMC2827561
OpenAlexW1976140509

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.