Evidence map›Paper›PMID 12400005›Full record

ArticleOncogene2002

RACK1: a novel substrate for the Src protein-tyrosine kinase.

Betty Y Chang, Rachel A Harte, Christine A Cartwright

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

57 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Dual functions of Rack1 in regulating Hedgehog pathway.Cell death and differentiation · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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
  13. Rack1 maintains intestinal homeostasis by protecting the integrity of the epithelial barrier.American journal of physiology. Gastrointestinal and liver physiology · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Betty Y ChangDepartment of Medicine, Stanford University, Stanford, California, CA 94305, USA.
Rachel A Harte
Christine A Cartwright
Stanford University · US

Funding

INTESTINAL CELL GROWTH CONTROL: ROLE OF TYROSINE KINASESR01DK043743 · NIDDK · STANFORD UNIVERSITY · PI CARTWRIGHT, CHRISTINE ANN · 1996 to 2015
$4.3M
IDENTIFICATION AND ANALYSIS OF SRC-BINDING PROTEINF32CA069810 · NCI · STANFORD UNIVERSITY · PI CHANG, BETTY YUCHING · 1996 to 1998
–
NCI NIH HHS CA69810NIDDK NIH HHS R01 DK43743
6 · The paper itself

Abstract

RACK1 is one of a group of PKC-interacting proteins collectively called RACKs (Receptors for Activated C-Kinases). Previously, we showed that RACK1 also interacts with the Src tyrosine kinase, and is an inhibitor of Src activity and cell growth. PKC activation induces the intracellular movement and co-localization of RACK1 and Src, and the tyrosine phosphorylation of RACK1. To determine whether RACK1 is a Src substrate, we assessed phosphorylation of RACK1 by various tyrosine kinases in vitro, and by kinase-active and inactive mutants of Src in vivo. We found that RACK1 is a Src substrate. Moreover, Src activity is necessary for both the tyrosine phosphorylation of RACK1 and the binding of RACK1 to Src's SH2 domain that occur following PKC activation. To identify the tyrosine(s) on RACK1 that is phosphorylated by Src, we generated and tested a series of RACK1 mutants. We found that Src phosphorylates RACK1 on Tyr 228 and/or Tyr 246, highly-conserved tyrosines located in the sixth WD repeat that interact with Src's SH2 domain. We think that RACK1 is an important Src substrate that signals downstream of growth factor receptor tyrosine kinases and is involved in the regulation of Src function and cell growth.

Indexed as

3T3 CellsAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCHO CellsCricetinaeErbB ReceptorsMiceMolecular Sequence DataOncogene Proteins v-ablPhosphorylationProtein Kinase CReceptors, Cell SurfaceReceptors for Activated C KinaseReceptors, Platelet-Derived Growth FactorErbB ReceptorsOncogene Proteins v-ablProtein Kinase CReceptors, Cell SurfaceReceptors for Activated C KinaseReceptors, Platelet-Derived Growth Factorsrc-Family KinasesTyrosine

Identifiers

PMID12400005
OpenAlexW2081048050

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.