Evidence map›Paper›PMID 12578912›Full record

ArticleThe Journal of cell biology2003

Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin.

Qiang Wang, Yi Xie, Quan-Sheng Du, Xiao-Jun Wu, Xu Feng, Lin Mei, Jay M McDonald, Wen-Cheng Xiong

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

46 citing papers in PubMed, 113 citations in OpenAlex.

  1. Trial
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  5. Article
  6. Water Extract of DesaltedNutrients · 2023
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  13. Specific RANK Cytoplasmic Motifs Drive Osteoclastogenesis.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2019
    Article
  14. Article
  15. The Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Adseverin knockdown inhibits osteoclastogenesis in RAW264.7 cells.International journal of molecular medicine · 2014
    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

8 authors at 1 institution in 1 country.

Qiang WangDepartment of Neurobiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Yi Xie
Quan-Sheng Du
Xiao-Jun Wu
Xu Feng
Lin Mei
Jay M McDonald
Wen-Cheng Xiong
University of Alabama at Birmingham · US

Funding

UAB Core Center for Musculoskeletal DisordersP30AR046031 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI GILBERT, SHAWN ROBERT · 2001 to 2010
$5.6M
RANK Signaling in Osteoclast Differentiation &FunctionR01AR047830 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FENG, XU · 2001 to 2016
$4.7M
SIGNALING MECHANISMS REGULATING ACHR SYNTHESIS AT NMJR01NS040480 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MEI, LIN · 2000 to 2013
$3.6M
ROLE OF PYK2 IN REGULATING OSTEOCLASTIC BONE RESORPTIONR01AR048120 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI XIONG, WEN-CHENG · 2002 to 2011
$2.5M
TAMOXIFEN MODULATES OSTEOCLAST CA++/CALMODULIN SIGNALINGR01AR043225 · NIAMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MCDONALD, JAY M · 1995 to 2001
$455k
NIAMS NIH HHS AR43225NIAMS NIH HHS AR46031NIAMS NIH HHS AR47830NIAMS NIH HHS AR48120NIAMS NIH HHS P30 AR046031NIAMS NIH HHS P30AR46031NIAMS NIH HHS R01 AR043225NIAMS NIH HHS R01 AR047830NIAMS NIH HHS R01 AR048120NINDS NIH HHS NS40480NINDS NIH HHS R01 NS040480
6 · The paper itself

Abstract

Osteoclast activation is important for bone remodeling and is altered in multiple bone disorders. This process requires cell adhesion and extensive actin cytoskeletal reorganization. Proline-rich tyrosine kinase 2 (PYK2), a major cell adhesion-activated tyrosine kinase in osteoclasts, plays an important role in regulating this event. The mechanisms by which PYK2 regulates actin cytoskeletal organization and osteoclastic activation remain largely unknown. In this paper, we provide evidence that PYK2 directly interacts with gelsolin, an actin binding, severing, and capping protein essential for osteoclastic actin cytoskeletal organization. The interaction is mediated via the focal adhesion-targeting domain of PYK2 and an LD motif in gelsolin's COOH terminus. PYK2 phosphorylates gelsolin at tyrosine residues and regulates gelsolin bioactivity, including decreasing gelsolin binding to actin monomer and increasing gelsolin binding to phosphatidylinositol lipids. In addition, PYK2 increases actin polymerization at the fibroblastic cell periphery. Finally, PYK2 interacts with gelsolin in osteoclasts, where PYK2 activation is required for the formation of actin rings. Together, our results suggest that PYK2 is a regulator of gelsolin, revealing a novel PYK2-gelsolin pathway in regulating actin cytoskeletal organization in multiple cells, including osteoclasts.

Indexed as

ActinsAmino Acid MotifsAnimalsCell AdhesionCell LineCytoskeletonFibroblastsFluorescent DyesFocal Adhesion Kinase 2GelsolinHumansMiceMice, KnockoutOsteoclastsPhalloidinePhosphatidylinositol 4,5-DiphosphateActinsFluorescent DyesFocal Adhesion Kinase 2GelsolinPhalloidinePhosphatidylinositol 4,5-DiphosphateProtein-Tyrosine KinasesPtk2b protein, mouseRecombinant Fusion Proteins

Identifiers

PMID12578912
PMCPMC2173747
OpenAlexW2120251787

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.