Evidence map›Paper›PMID 23723069›Full record

ArticleThe Journal of biological chemistry2013

Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3).

Hanine Rafidi, Francisco Mercado, Michael Astudillo, William H D Fry, Matthew Saldana, Kermit L Carraway, Colleen Sweeney

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  14. Glycosylation Changes in Brain Cancer.ACS chemical neuroscience · 2018
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. LRIG and cancer prognosis.Acta oncologica (Stockholm, Sweden) · 2014
    Review
  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

7 authors at 1 institution in 1 country.

Hanine RafidiDepartment of Biochemistry and Molecular Medicine, University of California at Davis Comprehensive Cancer Center, Sacramento, California 95817, USA.
Francisco Mercado
Michael Astudillo
William H D Fry
Matthew Saldana
Kermit L Carraway
Colleen Sweeney
University of California, Davis · US

Funding

NRDP1 PROTEIN DEGRADATION PATHWAY IN MAMMARY TUMOR PROGRESSIONR01CA123541 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CARRAWAY, KERMIT L · 2006 to 2016
$2.5M
Mechanisms of Receptor Tyrosine Kinase InhibitionR01CA118384 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SWEENEY, COLLEEN ANN · 2006 to 2016
$2.4M
NCI NIH HHS CA118384NCI NIH HHS CA123541NCI NIH HHS R01 CA118384NCI NIH HHS R01 CA123541
6 · The paper itself

Abstract

Lrig1 is the founding member of the Lrig family of transmembrane leucine-rich repeat proteins, which also includes Lrig2 and Lrig3. Lrig1 is a negative regulator of oncogenic receptor tyrosine kinases, including ErbB and Met receptors, and promotes receptor degradation. Lrig1 has recently emerged as both a tumor suppressor and a key regulator of epidermal and epithelial stem cell quiescence. Despite this, little is known of the mechanisms by which Lrig1 is regulated. Lrig3 was recently reported to increase ErbB receptor expression suggesting that it may function in a manner opposite to Lrig1. In this study, we explore the interaction between Lrig1 and Lrig3 and demonstrate that Lrig1 and Lrig3 functionally oppose one another. Lrig3 opposes Lrig1 negative regulatory activity and stabilizes ErbB receptors. Conversely, Lrig1 destabilizes Lrig3, limiting Lrig3's positive effects on receptors and identifying Lrig3 as a new target of Lrig1. These studies provide new insight into the regulation of Lrig1 and uncover a complex cross-talk between Lrig1 and Lrig3.

Indexed as

AnimalsBlotting, WesternCell Line, TumorCHO CellsCricetinaeCricetulusEndocytosisErb-b2 Receptor Tyrosine KinasesErbB ReceptorsHEK293 CellsHumansMCF-7 CellsMembrane GlycoproteinsMembrane ProteinsMutationProtein BindingERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesERBB3 protein, humanERBB4 protein, humanErbB ReceptorsLRIG1 protein, humanLRIG3 protein, humanMembrane GlycoproteinsMembrane ProteinsReceptor, ErbB-3Receptor, ErbB-4Epidermal Growth Factor Receptor (EGFR)Growth FactorLrig1Lrig3Protein DegradationReceptor Tyrosine KinaseSignal TransductionTumor Suppressor Gene

Identifiers

PMID23723069
PMCPMC3724619
OpenAlexW2029595157

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.