Evidence map›Paper›PMID 19592636›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2009

Casein kinase 2beta as a novel enhancer of activin-like receptor-1 signaling.

Nam Y Lee, John C Haney, Julie Sogani, Gerard C Blobe

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. BMP Signalling at the Crossroad of Liver Fibrosis and Regeneration.International journal of molecular sciences · 2017
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. TGFβ signaling and cardiovascular diseases.International journal of biological sciences · 2012
    Review
  11. Article
  12. CK2α is essential for embryonic morphogenesis.Molecular and cellular biochemistry · 2011
    Article
  13. Article
  14. 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

4 authors at 1 institution in 1 country.

Nam Y LeeDepartment of Medicine, Duke University, Durham, NC, USA.
John C Haney
Julie Sogani
Gerard C Blobe
Duke University · US

Funding

Translational Research in Surgical OncologyT32CA093245 · NCI · DUKE UNIVERSITY · PI ALLEN, PETER J, HARPOLE, DAVID H. · 2002 to 2020
$5.2M
ALK-1 and Endoglin Signaling in Endothelial CellsR01CA105255 · NCI · DUKE UNIVERSITY · PI BLOBE, GERARD C · 2004 to 2008
$1.5M
Novel Roles for beta-arrestin2 in TGF-beta mediated Endoglin SignalingF32CA124139 · NCI · DUKE UNIVERSITY · PI LEE, NAM Y · 2008 to 2009
$101k
NCI NIH HHS F32 CA124139NCI NIH HHS F32-CA124139NCI NIH HHS R01 CA105255NCI NIH HHS R01-CA105255NCI NIH HHS T32 CA093245NCI NIH HHS T32-CA093245
6 · The paper itself

Abstract

ALK-1 is a transforming growth factor beta (TGF-beta) superfamily receptor that is predominantly expressed in endothelial cells and is essential for angiogenesis, as demonstrated by the embryonic lethal phentoype when targeted for deletion in mice and its mutation in the human disease hereditary hemorrhagic telangiectasia. Although ALK-1 and the endothelial-specific TGF-beta superfamily coreceptor, endoglin, form a heteromeric complex and bind similar TGF-beta superfamily ligands, their signaling mechanisms remain poorly characterized. Here we report the identification of CK2beta, the regulatory subunit of protein kinase CK2, as a novel enhancer of ALK-1 signaling. The cytoplasmic domain of ALK-1 specifically binds to CK2beta in vitro and in vivo. NAAIRS mutagenesis studies define amino acid sequences 181-199 of CK2beta and 207-212 of ALK-1 as the interaction domains, respectively. The ALK-1/CK2beta interaction specifically enhanced Smad1/5/8 phosphorylation and ALK-1-mediated reporter activation in response to TGF-beta1 and BMP-9 treatment. In a reciprocal manner, siRNA-mediated silencing of endogenous CK2beta inhibited TGF-beta1 and BMP-9-stimulated Smad1/5/8 phosphorylation and ALK-1-mediated reporter activation. Functionally, CK2beta enhanced the ability of activated or ligand-stimulated ALK-1 to inhibit endothelial cell migration. Similarly, ALK-1 and CK2beta antagonized endothelial tubule formation in Matrigel. These studies support CK2beta as an important regulator of ALK-1 signaling and ALK-1-mediated functions in endothelial cells.

Indexed as

Activin Receptors, Type IIAnimalsCasein Kinase IIChlorocebus aethiopsCOS CellsHumansProtein Structure, TertiaryProtein SubunitsSignal TransductionSmad ProteinsTwo-Hybrid System TechniquesActivin Receptors, Type IIACVRL1 protein, humanCasein Kinase IIProtein SubunitsSmad Proteins

Identifiers

PMID19592636
PMCPMC2775003
OpenAlexW2053617247

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.