ArticleThe international journal of biochemistry & cell biology2012
Dynamin and PTP-PEST cooperatively regulate Pyk2 dephosphorylation in osteoclasts.
Article in The international journal of biochemistry & cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Protein tyrosine phosphatases in skeletal development and diseases.Bone research · 2022Review
- Pyk2 deficiency enhances bone mass during midpalatal suture expansion.Orthodontics & craniofacial research · 2020Article
- The dynamin inhibitor dynasore inhibits bone resorption by rapidly disrupting actin rings of osteoclasts.Journal of bone and mineral metabolism · 2016Article
- Pyk2 and Megakaryocytes Regulate Osteoblast Differentiation and Migration Via Distinct and Overlapping Mechanisms.Journal of cellular biochemistry · 2016Article
- Late stages of the synchronized macrophage fusion in osteoclast formation depend on dynamin.The Biochemical journal · 2014Article
- Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts.Molecular biology of the cell · 2014Article
- Osteoblast differentiation and migration are regulated by dynamin GTPase activity.The international journal of biochemistry & cell biology · 2014Article
- Role of dynamin 2 in the disassembly of focal adhesions.Journal of molecular medicine (Berlin, Germany) · 2013Review
- Regulation of tumor cell migration by protein tyrosine phosphatase (PTP)-proline-, glutamate-, serine-,and threonine-rich sequence (PEST).Chinese journal of cancer · 2013Review
- Focal adhesion kinases in adhesion structures and disease.Journal of signal transduction · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Bone loss is caused by the dysregulated activity of osteoclasts which degrade the extracellular bone matrix. The tyrosine kinase Pyk2 is highly expressed in osteoclasts, and mice lacking Pyk2 exhibit an increase in bone mass, in part due to impairment of osteoclast function. Pyk2 is activated by phosphorylation at Y402 following integrin activation, but the mechanisms leading to Pyk2 dephosphorylation are poorly understood. In the current study, we examined the mechanism of action of the dynamin GTPase on Pyk2 dephosphorylation. Our studies reveal a novel mechanism for the interaction of Pyk2 with dynamin, which involves the binding of Pyk2's FERM domain with dynamin's plextrin homology domain. In addition, we demonstrate that the dephosphorylation of Pyk2 requires dynamin's GTPase activity and is mediated by the tyrosine phosphatase PTP-PEST. The dephosphorylation of Pyk2 by dynamin and PTP-PEST may be critical for terminating outside-in integrin signaling, and for stabilizing cytoskeletal reorganization during osteoclast bone resorption.
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Registered trials
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.