Evidence map›Paper›PMID 22298426›Full record

ArticleMolecular biology of the cell2012

Phosphorylation of Stim1 at serine 575 via netrin-2/Cdo-activated ERK1/2 is critical for the promyogenic function of Stim1.

Hye-Jin Lee, Gyu-Un Bae, Young-Eun Leem, Hyun-Kyung Choi, Tong Mook Kang, Hana Cho, Seong-Tae Kim, Jong-Sun Kang

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Ouabain-regulated phosphoproteome reveals molecular mechanisms for NaFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  6. Review
  7. Article
  8. Article
  9. A focus on extracellular CaExperimental & molecular medicine · 2017
    Review
  10. Article
  11. Keep Your Friends Close: Cell-Cell Contact and Skeletal Myogenesis.Cold Spring Harbor perspectives in biology · 2017
    Review
  12. Store-Operated CaCurrent molecular biology reports · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. The regulation of STIM1 by phosphorylation.Communicative & integrative biology · 2013
    Review
  17. Article
  18. Article
  19. 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

8 authors at 1 institution in 1 country.

Hye-Jin LeeDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Republic of Korea.
Gyu-Un Bae
Young-Eun Leem
Hyun-Kyung Choi
Tong Mook Kang
Hana Cho
Seong-Tae Kim
Jong-Sun Kang
Samsung (South Korea) · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The promyogenic cell surface molecule Cdo is required for activation of extracellular signal-regulated kinase (ERK) and nuclear factor of activated T cells c3 (NFATc3) induced by netrin-2 in myogenic differentiation. However, the molecular mechanism leading to NFATc3 activation is unknown. Stromal interaction molecule 1 (Stim1), an internal calcium sensor of the endoplasmic reticulum store, promotes myogenesis via activation of NFATc3. In this study we investigated the functional interaction between Cdo and Stim1 in myogenic differentiation. Overexpression and depletion of Stim1 enhanced or decreased myotube formation, respectively. Of interest, Stim1 protein levels were decreased in Cdo-deficient perinatal hindlimb muscles or primary myoblasts; this correlates with defective NFATc3 activation in Cdo(-/-) myoblasts upon differentiation. Forced activation of NFATc3 by overexpression of calcineurin restored differentiation of Cdo-depleted C2C12 myoblasts. Furthermore, Cdo and Stim1 formed a complex in 293T cells or in differentiating C2C12 myoblasts. The netrin-2-mediated NFATc3 activation was coincident with robust interactions between Cdo and Stim1 in myoblasts and the ERK-mediated Stim1 phosphorylation at serine 575. The serine 575 phosphorylation was enhanced in C2C12 cells upon differentiation, and the alanine substitution of serine 575 failed to restore differentiation of Stim1-depleted myoblasts. Taken together, the results indicate that cell adhesion signaling triggered by netrin-2/Cdo induces Stim1 phosphorylation at serine 575 by ERK, which promotes myoblast differentiation.

Indexed as

AnimalsBase SequenceCalcineurinCalcium ChannelsCell Adhesion MoleculesCell DifferentiationCell LineHEK293 CellsHumansMAP Kinase Signaling SystemMembrane GlycoproteinsMiceMice, KnockoutMultiprotein ComplexesMuscle DevelopmentMuscle Fibers, SkeletalCalcineurinCalcium ChannelsCdon protein, mouseCell Adhesion MoleculesMembrane GlycoproteinsMultiprotein ComplexesNerve Growth Factorsnetrin-2NetrinsNfatc3 protein, mouseNFATC Transcription FactorsRNA, Small InterferingSerineStim1 protein, mouseStromal Interaction Molecule 1

Identifiers

PMID22298426
PMCPMC3315807
OpenAlexW2159661977

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.