Evidence map›Paper›PMID 17574549›Full record

ArticleExperimental cell research2007

RACK1 regulates Src activity and modulates paxillin dynamics during cell migration.

Ashley T Doan, Anna Huttenlocher

Open access · greenAbstract read
In one paragraph

Article in Experimental cell research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Apoptotic, Angiogenic and Cell Proliferation Genes CD63, S100A6 e GNB2L1 are Altered in Patients with Endometriosis.Revista brasileira de ginecologia e obstetricia : revista da Federacao Brasileira das Sociedades de Ginecologia e Obstetricia · 2018
    Article
  6. Article
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  8. Article
  9. Review
  10. Article
  11. RACK1 promoted the growth and migration of the cancer cells in the progression of esophageal squamous cell carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013
    Article
  12. Review
  13. RACK1 to the future--a historical perspective.Cell communication and signaling : CCS · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. RACK1, A multifaceted scaffolding protein: Structure and function.Cell communication and signaling : CCS · 2011
    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

2 authors at 1 institution in 1 country.

Ashley T DoanDepartment of Pharmacology, University of Wisconsin, Medical Sciences Center, Madison, WI 53706, USA.
Anna Huttenlocher
University of Wisconsin–Madison · US

Funding

ADHESIVE REGULATION DURING CELL MIGRATIONR01CA085862 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI Anna Huttenlocher · 2000 to 2026
$7.3M
NCI NIH HHS R01 CA085862NCI NIH HHS R01CA85862-06
6 · The paper itself

Abstract

Receptor for Activated C Kinase, RACK1, is an adaptor protein that regulates signaling via Src and PKC-dependent pathways, and has been implicated in cell migration. In this study we demonstrate novel functions for RACK1 in regulating adhesion dynamics during cell migration. We report that cells lacking RACK1 are less motile and show reduced dynamics of paxillin and talin at focal complexes. To investigate the role of the RACK1/Src interactions in adhesion dynamics, we used RACK1 in which the putative Src binding site has been mutated (RACK Y246F). RACK1-deficient cells showed enhanced c-Src activity that was rescued by expression of wild type RACK1, but not by RACK Y246F. Expression of wild type RACK1, but not RACK Y246F, was also able to rescue the adhesion and migration defects observed in the RACK1-deficient cells. Furthermore, our findings indicate that RACK1 functions to regulate paxillin phosphorylation and that its effects on paxillin dynamics require the Src-mediated phosphorylation of tyrosine 31/118 on paxillin. Taken together, these findings support a novel role for RACK1 as a key regulator of cell migration and adhesion dynamics through the regulation of Src activity, and the modulation of paxillin phosphorylation at early adhesions.

Indexed as

Cell MovementCell LineEnzyme ActivationFocal AdhesionsGTP-Binding ProteinsHumansNeoplasm ProteinsPaxillinPhosphorylationPhosphotyrosineProto-Oncogene Proteins pp60(c-src)Receptors, Cell SurfaceReceptors for Activated C KinaseGTP-Binding ProteinsNeoplasm ProteinsPaxillinPhosphotyrosineProto-Oncogene Proteins pp60(c-src)RACK1 protein, humanReceptors, Cell SurfaceReceptors for Activated C Kinase

Identifiers

PMID17574549
PMCPMC2679865
OpenAlexW1993878658

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.