Evidence map›Paper›PMID 18378693›Full record

ArticleMolecular and cellular biology2008

Phospholipase Cgamma2 modulates integrin signaling in the osteoclast by affecting the localization and activation of Src kinase.

Holly Epple, Viviana Cremasco, Kaihua Zhang, Dailing Mao, Gregory D Longmore, Roberta Faccio

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Anti-Osteoporotic Effects ofMolecules (Basel, Switzerland) · 2021
    Article
  5. Article
  6. Article
  7. Phospholipase C.Advances in experimental medicine and biology · 2020
    Review
  8. Osteoclast Signal Transduction During Bone Metastasis Formation.Frontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Alternative NF-κB Regulates RANKL-Induced Osteoclast Differentiation and Mitochondrial Biogenesis via Independent Mechanisms.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2015
    Article
  15. Diacylglycerol Kinase ζ (DGKζ) Is a Critical Regulator of Bone Homeostasis Via Modulation of c-Fos Levels in Osteoclasts.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Holly EppleWashington University School of Medicine, Department of Medicine, 660 South Euclid, St. Louis, MO 63110, USA.
Viviana Cremasco
Kaihua Zhang
Dailing Mao
Gregory D Longmore
Roberta Faccio
Washington University in St. Louis · US

Funding

The Role of LIM Proteins in Cell Migration and AdhesionR01CA085839 · NCI · WASHINGTON UNIVERSITY · PI LONGMORE, GREGORY D. · 2000 to 2009
$2.2M
NCI NIH HHS CA85839NCI NIH HHS R01 CA085839NIAMS NIH HHS R01 AR52921PHS HHS T32 07088
6 · The paper itself

Abstract

Integrin engagement induces a cascade of signaling pathways that include tyrosine phosphorylation of numerous proteins that lead to modulation of the actin cytoskeleton. Src is a major intracellular mediator of integrin-dependent functions, but the mechanism(s) by which Src is regulated in response to integrin signals is not fully understood. Here, we demonstrate an important role for phospholipase C gamma 2 (PLCgamma2) in Src activation in the osteoclast. Through analysis of primary cells from PLCgamma2(-/-) mice, PLCgamma2 was found to be an important regulator of alpha(v)beta(3) integrin-mediated bone osteoclast cell adhesion, migration, and bone resorption. Adhesion-induced PYK2 and Src phosphorylation is decreased in the absence of PLCgamma2, and the interaction of Src with beta(3) integrin and PYK2 is dramatically reduced. Importantly, PLCgamma2 was found to be required for proper localization of Src to the sealing actin ring, and this function required both its catalytic activity and adapter domains. Based on these results, we propose that PLCgamma2 influences Src activation by mediating the localization of Src to the integrin complex and thereby regulating integrin-mediated functions in the osteoclast.

Indexed as

ActinsAnimalsBone ResorptionCatalysisCell AdhesionCell DifferentiationCell MovementCells, CulturedFocal Adhesion Kinase 2Integrin alphaVIntegrin beta3MiceMice, Mutant StrainsNFATC Transcription FactorsOsteoclastsPhospholipase C gammaActinsFocal Adhesion Kinase 2Integrin alphaVIntegrin beta3Nfatc1 protein, mouseNFATC Transcription FactorsPhospholipase C gammaPtk2b protein, mousesrc-Family Kinases

Identifiers

PMID18378693
PMCPMC2423304
OpenAlexW2166838827

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.