Evidence map›Paper›PMID 9786953›Full record

ArticleThe Journal of cell biology1998

Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles.

M L Borowsky, R O Hynes

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

49 citing papers in PubMed, 160 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Review
  5. Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. PI(4,5)PAdvances in experimental medicine and biology · 2023
    Article
  13. Review
  14. Article
  15. Review
  16. Layilin Anchors Regulatory T Cells in Skin.Journal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  17. Article
  18. T-Cell Adhesion in Healthy and Inflamed Skin.JID innovations : skin science from molecules to population health · 2021
    Review
  19. Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020
    Review
  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 2 institutions in 1 country.

M L BorowskyHoward Hughes Medical Institute, Center for Cancer Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
R O Hynes
Howard Hughes Medical Institute · USMassachusetts Institute of Technology · US

Funding

CELL-SURFACE STRUCTURE AND TRANSFORMATIONSR01CA017007 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HYNES, RICHARD O · 1985 to 2005
$2.9M
NCI NIH HHS R01 CA017007NCI NIH HHS R01 CA17007
6 · The paper itself

Abstract

Changes in cell morphology and motility are mediated by the actin cytoskeleton. Recent advances in our understanding of the regulators of microfilament structure and dynamics have shed light on how these changes are controlled, and efforts continue to define all the structural and signaling components involved in these processes. The actin cytoskeleton-associated protein talin binds to integrins, vinculin, and actin. We report a new binding partner for talin that we have named layilin, which contains homology with C-type lectins, is present in numerous cell lines and tissue extracts, and is expressed on the cell surface. Layilin colocalizes with talin in membrane ruffles, and is recruited to membrane ruffles in cells induced to migrate in in vitro wounding experiments and in peripheral ruffles in spreading cells. A ten-amino acid motif in the layilin cytoplasmic domain is sufficient for talin binding. We have identified a short region within talin's amino-terminal 435 amino acids capable of binding to layilin in vitro. This region overlaps a binding site for focal adhesion kinase.

Indexed as

Amino Acid SequenceAnimalsCarrier ProteinsCell Adhesion MoleculesCHO CellsCricetinaeFemaleFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGlycoproteinsIntegrinsLectinsMembrane GlycoproteinsMembrane ProteinsMiceMolecular Sequence DataCarrier ProteinsCell Adhesion MoleculesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGlycoproteinsIntegrinslayilin protein, mouseLectinsMembrane GlycoproteinsMembrane ProteinsProtein-Tyrosine KinasesPtk2 protein, mouseRecombinant Fusion ProteinsRNA, MessengerTalin

Identifiers

PMID9786953
PMCPMC2132847
OpenAlexW2065642272

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.