Evidence map›Paper›PMID 11724822›Full record

ArticleThe Journal of cell biology2001

Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF.

S Taya, N Inagaki, H Sengiku, H Makino, A Iwamatsu, I Urakawa, K Nagao, S Kataoka, K Kaibuchi

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
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  5. Molecular Regulators of Cellular Mechanoadaptation at Cell-Material Interfaces.Frontiers in bioengineering and biotechnology · 2020
    Review
  6. Resistance protein Pit interacts with the GEF OsSPK1 to activate OsRac1 and trigger rice immunity.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
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  10. Review
  11. Article
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  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Non-canonical functions of RGS proteins.Cellular signalling · 2010
    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

9 authors at 3 institutions in 1 country.

S TayaDepartment of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya 466-8550, Japan.
N Inagaki
H Sengiku
H Makino
A Iwamatsu
I Urakawa
K Nagao
S Kataoka
K Kaibuchi
Kirin (Japan) · JPNagoya University · JPNara Institute of Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insulin-like growth factor (IGF)-1 plays crucial roles in growth control and rearrangements of the cytoskeleton. IGF-1 binds to the IGF-1 receptor and thereby induces the autophosphorylation of this receptor at its tyrosine residues. The phosphorylation of the IGF-1 receptor is thought to initiate a cascade of events. Although various signaling molecules have been identified, they appear to interact with the tyrosine-phosphorylated IGF-1 receptor. Here, we identified leukemia-associated Rho guanine nucleotide exchange factor (GEF) (LARG), which contains the PSD-95/Dlg/ZO-1 (PDZ), regulator of G protein signaling (RGS), Dbl homology, and pleckstrin homology domains, as a nonphosphorylated IGF-1 receptor-interacting molecule. LARG formed a complex with the IGF-1 receptor in vivo, and the PDZ domain of LARG interacted directly with the COOH-terminal domain of IGF-1 receptor in vitro. LARG had an exchange activity for Rho in vitro and induced the formation of stress fibers in NIH 3T3 fibroblasts. When MDCKII epithelial cells were treated with IGF-1, Rho and its effector Rho-associated kinase (Rho-kinase) were activated and actin stress fibers were enhanced. Furthermore, the IGF-1-induced Rho-kinase activation and the enhancement of stress fibers were inhibited by ectopic expression of the PDZ and RGS domains of LARG. Taken together, these results indicate that IGF-1 activates the Rho/Rho-kinase pathway via a LARG/IGF-1 receptor complex and thereby regulates cytoskeletal rearrangements.

Indexed as

Amino Acid SequenceAnimalsCell LineGenes, ReporterGuanine Nucleotide Exchange FactorsHumansImmunoblottingInsulin-Like Growth Factor IMiceMolecular Sequence DataProtein Structure, TertiaryRatsReceptor, IGF Type 1Recombinant Fusion Proteinsrho GTP-Binding ProteinsRho Guanine Nucleotide Exchange FactorsARHGEF12 protein, humanArhgef12 protein, mouseGuanine Nucleotide Exchange FactorsInsulin-Like Growth Factor IReceptor, IGF Type 1Recombinant Fusion Proteinsrho GTP-Binding ProteinsRho Guanine Nucleotide Exchange Factors

Identifiers

PMID11724822
PMCPMC2150867
OpenAlexW2102010710

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.