Evidence map›Paper›PMID 32182705›Full record

ArticleCells2020

Stimulation of Fibronectin Matrix Assembly by Lysine Acetylation.

Maria E Vega, Birgit Kastberger, Bernhard Wehrle-Haller, Jean E Schwarzbauer

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

20 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Fibronectin matrix assembly at a glance.Journal of cell science · 2025
    Review
  8. Review
  9. Review
  10. Mechanisms of assembly and remodelling of the extracellular matrix.Nature reviews. Molecular cell biology · 2024
    Review
  11. Article
  12. Article
  13. Review
  14. Implications of fibrotic extracellular matrix in diabetic retinopathy.Experimental biology and medicine (Maywood, N.J.) · 2022
    Review
  15. Article
  16. Review
  17. Article
  18. Roles of Integrins in Gastrointestinal Cancer Metastasis.Frontiers in molecular biosciences · 2021
    Review
  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

4 authors at 1 institution in 1 country.

Maria E VegaDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.ORCID 0000-0003-3190-1752
Birgit KastbergerDepartment of Cell Physiology and Metabolism, Centre Médical Universitaire, 1 Rue Michel-Servet, CMU, 1211 Geneva 4, Switzerland.
Bernhard Wehrle-HallerDepartment of Cell Physiology and Metabolism, Centre Médical Universitaire, 1 Rue Michel-Servet, CMU, 1211 Geneva 4, Switzerland.ORCID 0000-0002-1159-1147
Jean E SchwarzbauerDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.ORCID 0000-0003-1012-7593
Princeton University · US

Funding

Fibronectin-dependent mechanisms governing the assembly of a definitive extracellular matrixR01AR073236 · NIAMS · PRINCETON UNIVERSITY · PI SCHWARZBAUER, JEAN E · 2018 to 2022
$1.7M
Mechanisms of high glucose induced fibronectin matrix assembly by mesangial cells.F32DK109622 · NIDDK · PRINCETON UNIVERSITY · PI VEGA, MARIA EUGENIA · 2016 to 2018
$178k
NIAMS NIH HHS R01 AR073236NIDDK NIH HHS F32 DK109622
6 · The paper itself

Abstract

Diabetic nephropathy, a devastating consequence of diabetes mellitus, is characterized by the accumulation of extracellular matrix (ECM) that disrupts the kidney's filtration apparatus. Elevated glucose levels increase the deposition of a fibronectin (FN) matrix by mesangial cells, the primary matrix-producing cells of the kidney, and also increase acetyl-CoA leading to higher levels of lysine acetylation. Here, we investigated the connection between acetylation and the ECM and show that treatment of mesangial cells with deacetylase inhibitors increases both acetylation and FN matrix assembly compared to untreated cells. The matrix effects were linked to lysine 794 (K794) in the β1 integrin cytoplasmic domain based on studies of cells expressing acetylated (K794Q) and non-acetylated (K794R) mimetics. β1(K794Q) cells assembled significantly more FN matrix than wildtype β1 cells, while the non-acetylated β1(K794R) form was inactive. We show that mutation of K794 affects FN assembly by stimulating integrin-FN binding activity and cell contractility. Wildtype and β1(K794Q) cells but not β1(K794R) cells further increased their FN matrix when stimulated with deacetylase inhibitors indicating that increased acetylation on other proteins is required for maximum FN assembly. Thus, lysine acetylation provides a mechanism for glucose-induced fibrosis by up-regulation of FN matrix assembly.

Indexed as

AcetylationAnimalsDiabetic NephropathiesExtracellular MatrixFibronectinsHumansLysineMiceFibronectinsLysinediabetic nephropathyextracellular matrixfibronectinfibrosiskindlin-2β1 integrin

Identifiers

PMID32182705
PMCPMC7140634
OpenAlexW3010257400

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.