Evidence map›Paper›PMID 24005669›Full record

ArticleThe Journal of biological chemistry2013

Proteomic profiling of endothelial invasion revealed receptor for activated C kinase 1 (RACK1) complexed with vimentin to regulate focal adhesion kinase (FAK).

Jui M Dave, Hojin Kang, Colette A Abbey, Steve A Maxwell, Kayla J Bayless

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
2.8field-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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. SRC and ERK Regulate the Turnover of Cytoskeletal Keratin Filaments.International journal of molecular sciences · 2025
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  12. Selective regulation of Notch ligands during angiogenesis is mediated by vimentin.Proceedings of the National Academy of Sciences of the United States of America · 2017
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  15. Intermediate filament dynamics: What we can see now and why it matters.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
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  19. Microtubule-dependent transport of vimentin filament precursors is regulated by actin and by the concerted action of Rho- and p21-activated kinases.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  20. Review
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.

Jui M DaveFrom the Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas 77843.
Hojin KangFrom the Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas 77843.
Colette A AbbeyFrom the Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas 77843.
Steve A MaxwellFrom the Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas 77843.
Kayla J BaylessFrom the Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, Texas 77843. Electronic address: kbayless@medicine.tamhsc.edu.
Texas A&M Health Science Center · US

Funding

Mechanisms of Angiogenic Switch Activation During Wound RepairR01HL095786 · NHLBI · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI BAYLESS, KAYLA J · 2010 to 2014
$1.8M
NHLBI NIH HHS HL-095786NHLBI NIH HHS R01 HL095786
6 · The paper itself

Abstract

Angiogenesis is critical for many physiological and pathological processes. To identify molecules relevant to angiogenesis, we performed a proteomic screen comparing invading versus non-invading endothelial cells in three-dimensional collagen matrices. We found up-regulated levels of receptor for activated C kinase 1 (RACK1) and the intermediate filament protein vimentin that correlated with increased endothelial cell invasion. Because both RACK1 and vimentin have been linked to focal adhesion kinase (FAK), we investigated whether this pathway regulated invasion. RACK1 depletion reduced invasion responses, and this was associated with attenuated activation of FAK. Knockdown of vimentin significantly decreased levels of phosphorylated and total FAK. Treatment with a pharmacological inhibitor of FAK dose-dependently reduced invasion, indicating a crucial role for FAK activity during invasion. Because RACK1 and vimentin were both up-regulated with sphingosine 1-phosphate treatment, required for invasion, and regulated FAK, we tested whether they complexed together. RACK1 complexed with vimentin, and growth factors enhanced this interaction. In addition, RACK1, vimentin, and FAK formed an intermolecular complex in invading endothelial cultures in three dimensions in response to stimulation by sphingosine 1-phosphate and growth factors. Moreover, depletion of RACK1 decreased the association of vimentin and FAK, suggesting that RACK1 was required for stabilizing vimentin-FAK interactions during sprouting. Silencing of vimentin and RACK1 decreased cell adhesion and focal contact formation. Taken together, these results demonstrate that proangiogenic signals converge to enhance expression and association of RACK1 and vimentin, which regulated FAK, resulting in successful endothelial sprout formation in three-dimensional collagen matrices.

Indexed as

CollagenEnzyme ActivationExtracellular MatrixFocal Adhesion Kinase 1Gene Expression Regulation, EnzymologicGene Knockdown TechniquesGTP-Binding ProteinsHumansHuman Umbilical Vein Endothelial CellsLysophospholipidsMultiprotein ComplexesNeoplasm ProteinsNeovascularization, PhysiologicPhosphotransferases (Alcohol Group Acceptor)Protein StabilityProteomicsCollagenFocal Adhesion Kinase 1GTP-Binding ProteinsLysophospholipidsMultiprotein ComplexesNeoplasm ProteinsPhosphotransferases (Alcohol Group Acceptor)PTK2 protein, humanRACK1 protein, humanReceptors, Cell SurfaceReceptors for Activated C KinaseSphingosinesphingosine 1-phosphateSphingosine KinaseVimentinAngiogenesisCollagenEndothelial CellFocal Adhesion KinaseMorphogenesisRACK1Vimentin

Identifiers

PMID24005669
PMCPMC3798542
OpenAlexW2091206873

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.