Evidence map›Paper›PMID 10613911›Full record

ArticleThe Journal of cell biology1999

Molecular dissection of zyxin function reveals its involvement in cell motility.

B E Drees, K M Andrews, M C Beckerle

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis.Frontiers in cell and developmental biology · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  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

3 authors at 1 institution in 1 country.

B E DreesDepartment of Biology, University of Utah, Salt Lake City, Utah 84112-5550, USA.
K M Andrews
M C Beckerle
University of Utah · US

Funding

Structure and function of stress fibers and cell adhesion sitesR01GM050877 · NIGMS · UNIVERSITY OF UTAH · PI BECKERLE, MARY C. · 1994 to 2020
$7.8M
NIGMS NIH HHS GM50877NIGMS NIH HHS R01 GM050877
6 · The paper itself

Abstract

Spatially controlled actin filament assembly is critical for numerous processes, including the vectorial cell migration required for wound healing, cell- mediated immunity, and embryogenesis. One protein implicated in the regulation of actin assembly is zyxin, a protein concentrated at sites where the fast growing ends of actin filaments are enriched. To evaluate the role of zyxin in vivo, we developed a specific peptide inhibitor of zyxin function that blocks its interaction with alpha-actinin and displaces it from its normal subcellular location. Mislocalization of zyxin perturbs cell migration and spreading, and affects the behavior of the cell edge, a structure maintained by assembly of actin at sites proximal to the plasma membrane. These results support a role for zyxin in cell motility, and demonstrate that the correct positioning of zyxin within the cell is critical for its physiological function. Interestingly, the mislocalization of zyxin in the peptide-injected cells is accompanied by disturbances in the distribution of Ena/VASP family members, proteins that have a well-established role in promoting actin assembly. In concert with previous work, our findings suggest that zyxin promotes the spatially restricted assembly of protein complexes necessary for cell motility.

Indexed as

Amino Acid SequenceAnimalsCell LineCell MovementCytoskeletal ProteinsDipodomysFibronectinsGlycoproteinsHumansMetalloproteinsMicroinjectionsMolecular Sequence DataPeptide FragmentsZyxinCytoskeletal ProteinsFibronectinsGlycoproteinsMetalloproteinsPeptide FragmentsZyxinZYX protein, human

Identifiers

PMID10613911
PMCPMC2174240
OpenAlexW2137079116

What OpenQuestion holds

Textmetadata
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.