Evidence map›Paper›PMID 30092354›Full record

ArticleCellular signalling2018

Cellular phosphatase activity of C1-Ten/Tensin2 is controlled by Phosphatidylinositol-3,4,5-triphosphate binding through the C1-Ten/Tensin2 SH2 domain.

Eui Kim, Do-Hyeon Kim, Indira Singaram, Heeyoon Jeong, Ara Koh, Jiyoun Lee, Wonhwa Cho, Sung Ho Ryu

Open access · greenAbstract read
In one paragraph

Article in Cellular signalling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. PI(3,5)PScience advances · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Tensins in Kidney Function and Diseases.Life (Basel, Switzerland) · 2023
    Review
  7. Lipid Binding of SH2 Domains.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Review
  9. Review
  10. Review
  11. Review
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

8 authors at 2 institutions in 2 countries.

Eui KimDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 37673, South Korea; Brain Korea 21 PLUS project of Bio-Molecular Function, Pohang University of Science and Technology, Pohang 37673, South Korea.
Do-Hyeon KimDepartment of Life Sciences, Pohang University of Science and Technology, Pohang 37673, South Korea.
Indira SingaramDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.
Heeyoon JeongDepartment of Life Sciences, Pohang University of Science and Technology, Pohang 37673, South Korea; Brain Korea 21 PLUS project of Bio-Molecular Function, Pohang University of Science and Technology, Pohang 37673, South Korea.
Ara KohDepartment of Life Sciences, Pohang University of Science and Technology, Pohang 37673, South Korea.
Jiyoun LeeDepartment of Life Sciences, Pohang University of Science and Technology, Pohang 37673, South Korea; Brain Korea 21 PLUS project of Bio-Molecular Function, Pohang University of Science and Technology, Pohang 37673, South Korea.
Wonhwa ChoDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA. Electronic address: wcho@uic.edu.
Sung Ho RyuDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 37673, South Korea; Department of Life Sciences, Pohang University of Science and Technology, Pohang 37673, South Korea; Brain Korea 21 PLUS project of Bio-Molecular Function, Pohang University of Science and Technology, Pohang 37673, South Korea. Electronic address: sungho@postech.ac.kr.
Pohang University of Science and Technology · KRUniversity of Illinois Chicago · US

Funding

Supplement for Equipment for Lipid Regulation of Cellular Signaling and Protein-Protein InteractionsR35GM122530 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI WONHWA CHO · 2017 to 2026
$6.1M
NIGMS NIH HHS R35 GM122530
6 · The paper itself

Abstract

Regulation of tyrosine phosphorylation on insulin receptor substrate-1 (IRS-1) is essential for insulin signaling. The protein tyrosine phosphatase (PTP) C1-Ten/Tensin2 has been implicated in the regulation of IRS-1, but the molecular basis of this dephosphorylation is not fully understood. Here, we demonstrate that the cellular phosphatase activity of C1-Ten/Tensin2 on IRS-1 is mediated by the binding of the C1-Ten/Tensin2 Src-homology 2 (SH2) domain to phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P

Indexed as

src Homology DomainsAnimalsEscherichia coliHEK293 CellsHumansInsulin Receptor Substrate ProteinsL CellsMiceMutagenesis, Site-DirectedPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphorylationPhosphotyrosineTensinsInsulin Receptor Substrate Proteinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphotyrosineTensinsTNS2 protein, humanC1-Ten/Tensin2Insulin receptor substrate-1Phosphatidylinositol-3,4,5-triphosphate bindingProtein tyrosine phosphataseSrc-homology 2 domain

Identifiers

PMID30092354
PMCPMC6392469
OpenAlexW2885885892

What OpenQuestion holds

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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.