Evidence map›Paper›PMID 10790367›Full record

ArticleThe EMBO journal2000

Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK.

M A del Pozo, L S Price, N B Alderson, X D Ren, M A Schwartz

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
17.7field-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

190 citing papers in PubMed, 447 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. A PAK family kinase and the Hippo/Yorkie pathway modulate WNT signaling to functionally integrate body axes during regeneration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Article
  8. Article
  9. Actin flow-dependent and -independent force transmission through integrins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Review
  13. Effect of PAK Inhibition on Cell Mechanics Depends on Rac1.Frontiers in cell and developmental biology · 2020
    Article
  14. Review
  15. SHOC2 complex-driven RAF dimerization selectively contributes to ERK pathway dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Review
  17. Article
  18. Integrin and microtubule crosstalk in the regulation of cellular processes.Cellular and molecular life sciences : CMLS · 2018
    Review
  19. Article
  20. Article

130 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

5 authors at 1 institution in 1 country.

M A del PozoDepartment of Vascular Biology, Scripps Research Institute, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA.
L S Price
N B Alderson
X D Ren
M A Schwartz
Scripps Research Institute · US

Funding

The Rho Family GTPases in Integrin SignalingR01GM047214 · NIGMS · YALE UNIVERSITY · PI SCHWARTZ, MARTIN A · 1991 to 2020
$6.3M
NIGMS NIH HHS R01 GM047214NIGMS NIH HHS R01 GM47214
6 · The paper itself

Abstract

The small GTPase Rac regulates cytoskeletal organization, cell cycle progression, gene expression and oncogenic transformation, processes that depend upon both soluble growth factors and adhesion to the extracellular matrix (ECM). We now show that growth factors and adhesion to the ECM both contribute independently and approximately equally to Rac activation. However, activated Rac in non-adherent cells failed to stimulate the Rac effector PAK. V12 Rac or Rac activated by serum translocated to the membrane fraction of adherent cells but remained mainly cytoplasmic in suspended cells. An activated Rac mutant lacking a membrane-targeting sequence did not activate PAK in adherent cells, while mutations that forced membrane targeting restored PAK activation in suspended cells. In vitro, V12 Rac showed greater binding to membranes from adherent relative to suspended cells, indicating that cell adhesion regulated membrane binding sites for Rac. These results show that ECM regulates the ability of Rac to couple with PAK via an effect on membrane binding sites that facilitate their interaction.

Indexed as

AnimalsBiological Transportcdc42 GTP-Binding ProteinCell AdhesionCell LineCell MembraneCulture Media, Serum-FreeCytoplasmEnzyme ActivationExtracellular MatrixFibronectinsGrowth SubstancesGuanosine TriphosphateIntegrinsMiceMutationcdc42 GTP-Binding ProteinCulture Media, Serum-FreeFibronectinsGrowth SubstancesGuanosine TriphosphateIntegrinsMyristic Acidp21-Activated KinasesPak1 protein, mousePak1 protein, ratProtein Serine-Threonine Kinasesrac GTP-Binding ProteinsRecombinant Fusion Proteins

Identifiers

PMID10790367
PMCPMC305684
OpenAlexW2114902150

What OpenQuestion holds

Textmetadata
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.