Evidence map›Paper›PMID 18678706›Full record

ArticleThe Journal of cell biology2008

A Cdo-Bnip-2-Cdc42 signaling pathway regulates p38alpha/beta MAPK activity and myogenic differentiation.

Jong-Sun Kang, Gyu-Un Bae, Min-Jeong Yi, Youn-Joo Yang, Ji-Eun Oh, Giichi Takaesu, Yi Ting Zhou, Boon Chuan Low, Robert S Krauss

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

64 citing papers in PubMed, 104 citations in OpenAlex.

  1. Review
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  9. Regulatory mechanisms of cytoneme-based morphogen transport.Cellular and molecular life sciences : CMLS · 2022
    Review
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  11. Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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4 more citing papers are in PubMed but not listed here.

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 3 countries.

Jong-Sun KangDepartment of Developmental and Regenerative Biology, Mount Sinai School of Medicine, New York, NY 10029, USA. jskang@med.skku.ac.kr
Gyu-Un Bae
Min-Jeong Yi
Youn-Joo Yang
Ji-Eun Oh
Giichi Takaesu
Yi Ting Zhou
Boon Chuan Low
Robert S Krauss
Icahn School of Medicine at Mount Sinai · USNational University of Singapore · SGSungkyunkwan University · KR

Funding

THE ROLE OF CDO IN MYOGENIC DIFFERENTIATIONR01AR046207 · NIAMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRAUSS, ROBERT S. · 2000 to 2015
$5.1M
NIAMS NIH HHS AR46207NIAMS NIH HHS R01 AR046207
6 · The paper itself

Abstract

The p38alpha/beta mitogen-activated protein kinase (MAPK) pathway promotes skeletal myogenesis, but the mechanisms by which it is activated during this process are unclear. During myoblast differentiation, the promyogenic cell surface receptor Cdo binds to the p38alpha/beta pathway scaffold protein JLP and, via JLP, p38alpha/beta itself. We report that Cdo also interacts with Bnip-2, a protein that binds the small guanosine triphosphatase (GTPase) Cdc42 and a negative regulator of Cdc42, Cdc42 GTPase-activating protein (GAP). Moreover, Bnip-2 and JLP are brought together through mutual interaction with Cdo. Gain- and loss-of-function experiments with myoblasts indicate that the Cdo-Bnip-2 interaction stimulates Cdc42 activity, which in turn promotes p38alpha/beta activity and cell differentiation. These results reveal a previously unknown linkage between a cell surface receptor and downstream modulation of Cdc42 activity. Furthermore, interaction with multiple scaffold-type proteins is a distinctive mode of cell surface receptor signaling and provides one mechanism for specificity of p38alpha/beta activation during cell differentiation.

Indexed as

Cell DifferentiationMuscle DevelopmentSignal TransductionAdaptor Proteins, Signal TransducingAnimalscdc42 GTP-Binding ProteinCell Adhesion MoleculesCell LineEnzyme ActivationGene DeletionHumansMiceMyoblastsp38 Mitogen-Activated Protein KinasesProtein BindingProteinsAdaptor Proteins, Signal Transducingcdc42 GTP-Binding ProteinCdon protein, mouseCell Adhesion MoleculesNip21 protein, mousep38 Mitogen-Activated Protein KinasesProteinsSpag9 protein, mouse

Identifiers

PMID18678706
PMCPMC2500135
OpenAlexW1992117085

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.