Evidence map›Paper›PMID 20547766›Full record

ArticleThe Journal of biological chemistry2010

c-Src-mediated phosphorylation of thyroid hormone receptor-interacting protein 6 (TRIP6) promotes osteoclast sealing zone formation.

Brooke K McMichael, Stephanie M Meyer, Beth S Lee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Autotaxin/Lysophosphatidic Acid Axis: From Bone Biology to Bone Disorders.International journal of molecular sciences · 2022
    Review
  5. Recent Advances in Osteoclast Biological Behavior.Frontiers in cell and developmental biology · 2021
    Review
  6. [Research progress on the biological regulatory function of lysophosphatidic acid in bone tissue cells].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2020
    Review
  7. Article
  8. Osteoblast-osteoclast interactions.Connective tissue research · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Brooke K McMichaelDepartment of Physiology and Cell Biology, The Ohio State University College of Medicine, Columbus, Ohio 43210, USA.
Stephanie M Meyer
Beth S Lee
The Ohio State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Osteoclasts resorb bone through the formation of a unique attachment structure called the sealing zone. In this study, a role for thyroid hormone receptor-interacting protein 6 (TRIP6) in sealing zone formation and osteoclast activity was examined. TRIP6 was shown to reside in the sealing zone through its association with tropomyosin 4, an actin-binding protein that regulates sealing dimensions and bone resorptive capacity. Suppression of TRIP6 in mature osteoclasts by RNA interference altered sealing zone dimensions and inhibited bone resorption, whereas overexpression of TRIP6 increased the sealing zone perimeter and enhanced bone resorption. Treatment of osteoclasts with lysophosphatidic acid (LPA), which phosphorylates TRIP6 at tyrosine 55 through a c-Src-dependent mechanism, caused increased association of TRIP6 with the sealing zone, as did overexpression of a TRIP6 cDNA bearing a phosphomimetic mutation at tyrosine 55. Further, LPA treatment caused increases in osteoclast fusion, sealing zone perimeter, and bone resorptive capacity. In contrast, overexpression of TRIP6 containing a nonphosphorylatable amino acid residue at position 55 severely diminished sealing zone formation and bone resorption and suppressed the effects of LPA on the cytoskeleton. LPA effects were mediated through its receptor isoform LPA(2), as indicated by treatments with receptor-specific agonists and antagonists. Thus, these studies suggest that TRIP6 is a critical downstream regulator of c-Src signaling and that its phosphorylation is permissive for its presence in the sealing zone where it plays a positive role in osteoclast bone resorptive capacity.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsATPases Associated with Diverse Cellular ActivitiesBone ResorptionCell FusionCSK Tyrosine-Protein KinaseLIM Domain ProteinsLysophospholipidsMiceOsteoclastsPhosphorylationProteasome Endopeptidase ComplexProtein-Tyrosine Kinasessrc-Family KinasesTranscription FactorsAdaptor Proteins, Signal TransducingATPases Associated with Diverse Cellular ActivitiesCSK protein, humanCSK Tyrosine-Protein KinaseLIM Domain Proteinslysophosphatidic acidLysophospholipidsProteasome Endopeptidase ComplexProtein-Tyrosine KinasesPSMC5 protein, humansrc-Family KinasesTranscription Factors

Identifiers

PMID20547766
PMCPMC2924104
OpenAlexW1983217851

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.