Evidence map›Paper›PMID 21454675›Full record

ArticleThe Journal of biological chemistry2011

Receptor-type protein tyrosine phosphatase beta (RPTP-beta) directly dephosphorylates and regulates hepatocyte growth factor receptor (HGFR/Met) function.

Yiru Xu, Wei Xia, Dustin Baker, Jin Zhou, Hyuk Chol Cha, John J Voorhees, Gary J Fisher

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Activation of FGF receptor signaling promotes invasion of non-small-cell lung cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  6. Article
  7. Review
  8. Inhibition of fibroblast growth factor receptor signaling impairs metastasis of hepatocellular carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  9. Article
  10. Article
  11. Article
  12. Iron and cancer: more ore to be mined.Nature reviews. Cancer · 2013
    Review
  13. Review
  14. 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

7 authors at 1 institution in 1 country.

Yiru XuDepartment of Dermatology, University of Michigan Medica School, Ann Arbor, MI 48109-5609, USA. xuyiru@umich.edu
Wei Xia
Dustin Baker
Jin Zhou
Hyuk Chol Cha
John J Voorhees
Gary J Fisher
University of Michigan–Ann Arbor · US

Funding

Receptor Protein Tyrosine Phosphatase-k Regulation of EGFRR01ES012920 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FISHER, GARY J, XU, YIRU · 2005 to 2015
$3.3M
NIEHS NIH HHS 5R01 ES012920NIEHS NIH HHS R01 ES012920
6 · The paper itself

Abstract

Protein tyrosine phosphorylation is a ubiquitous, fundamental biochemical mechanism that regulates essential eukaryotic cellular functions. The level of tyrosine phosphorylation of specific proteins is finely tuned by the dynamic balance between protein tyrosine kinase and protein tyrosine phosphatase activities. Hepatocyte growth factor receptor (also known as Met), a receptor protein tyrosine kinase, is a major regulator of proliferation, migration, and survival for many epithelial cell types. We report here that receptor-type protein tyrosine phosphatase β (RPTP-β) specifically dephosphorylates Met and thereby regulates its function. Expression of RPTP-β, but not other RPTP family members or catalytically inactive forms of RPTP-β, reduces hepatocyte growth factor (HGF)-stimulated Met tyrosine phosphorylation in HEK293 cells. Expression of RPTP-β in primary human keratinocytes reduces both basal and HGF-induced Met phosphorylation at tyrosine 1356 and inhibits downstream MEK1/2 and Erk activation. Furthermore, shRNA-mediated knockdown of endogenous RPTP-β increases basal and HGF-stimulated Met phosphorylation at tyrosine 1356 in primary human keratinocytes. Purified RPTP-β intracellular domain preferentially dephosphorylates purified Met at tyrosine 1356 in vitro. In addition, the substrate-trapping mutant of RPTP-β specifically interacts with Met in intact cells. Expression of RPTP-β in human primary keratinocytes reduces HGF induction of VEGF expression, proliferation, and motility. Taken together, the above data indicate that RPTP-β is a key regulator of Met function.

Indexed as

Cell ProliferationCell MovementGene Expression RegulationHEK293 CellsHumansKeratinocytesMAP Kinase Kinase 1MAP Kinase Kinase 2MutationPhosphorylationProto-Oncogene Proteins c-metReceptor-Like Protein Tyrosine Phosphatases, Class 5Receptors, Growth FactorVascular Endothelial Growth Factor AMAP2K1 protein, humanMAP2K2 protein, humanMAP Kinase Kinase 1MAP Kinase Kinase 2MET protein, humanProto-Oncogene Proteins c-metReceptor-Like Protein Tyrosine Phosphatases, Class 5Receptors, Growth FactorVascular Endothelial Growth Factor AVEGFA protein, human

Identifiers

PMID21454675
PMCPMC3091207
OpenAlexW1975503754

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.