Evidence map›Paper›PMID 10225961›Full record

ArticleThe Journal of cell biology1999

Laminin polymerization induces a receptor-cytoskeleton network.

H Colognato, D A Winkelmann, P D Yurchenco

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 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
8.1field-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

111 citing papers in PubMed, 303 citations in OpenAlex.

  1. Mechanisms of podocyte injury in genetic kidney disease.Pediatric nephrology (Berlin, Germany) · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Generating a Fractal Microstructure of Laminin-111 to Signal to Cells.Journal of visualized experiments : JoVE · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Alport syndrome and Pierson syndrome: Diseases of the glomerular basement membrane.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  17. Article
  18. Review
  19. Review
  20. Review

51 more citing papers are in PubMed but not listed here.

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.

H ColognatoDepartment of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
D A Winkelmann
P D Yurchenco
Johnson University · US

Funding

BASEMENT MEMBRANE SELF-ASSEMBLY &STRUCTURER01DK036425 · NIDDK · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI YURCHENCO, PETER DANA · 1986 to 2022
$4.3M
MOLECULAR PROBES OF MYOSIN STRUCTURE AND INTERACTIONSR01AR038454 · NIAMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI WINKELMANN, DONALD A · 1994 to 2008
$2.2M
NIAMS NIH HHS R01 AR038454NIAMS NIH HHS R01-AR38454NIDDK NIH HHS R01 DK036425NIDDK NIH HHS R01-DK36425
6 · The paper itself

Abstract

The transition of laminin from a monomeric to a polymerized state is thought to be a crucial step in the development of basement membranes and in the case of skeletal muscle, mutations in laminin can result in severe muscular dystrophies with basement membrane defects. We have evaluated laminin polymer and receptor interactions to determine the requirements for laminin assembly on a cell surface and investigated what cellular responses might be mediated by this transition. We found that on muscle cell surfaces, laminins preferentially polymerize while bound to receptors that included dystroglycan and alpha7beta1 integrin. These receptor interactions are mediated through laminin COOH-terminal domains that are spatially and functionally distinct from NH2-terminal polymer binding sites. This receptor-facilitated self-assembly drives rearrangement of laminin into a cell-associated polygonal network, a process that also requires actin reorganization and tyrosine phosphorylation. As a result, dystroglycan and integrin redistribute into a reciprocal network as do cortical cytoskeleton components vinculin and dystrophin. Cytoskeletal and receptor reorganization is dependent on laminin polymerization and fails in response to receptor occupancy alone (nonpolymerizing laminin). Preferential polymerization of laminin on cell surfaces, and the resulting induction of cortical architecture, is a cooperative process requiring laminin- receptor ligation, receptor-facilitated self-assembly, actin reorganization, and signaling events.

Indexed as

ActinsAnimalsCells, CulturedCytoskeletonHumansIntegrinsLamininMembrane ProteinsMiceMice, Mutant StrainsMuscle, SkeletalMuscular Dystrophy, AnimalPhosphorylationPolymersProtein Structure, TertiaryReceptors, LamininActinsintegrin alpha7beta1IntegrinsLamininlaminin alpha 2Membrane ProteinsPolymersReceptors, LamininTyrosine

Identifiers

PMID10225961
PMCPMC2185083
OpenAlexW1994556000

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.