ArticleMolecular and cellular biology2009
Dynamin reduces Pyk2 Y402 phosphorylation and SRC binding in osteoclasts.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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.
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Who cites it
32 citing papers in PubMed, 44 citations in OpenAlex.
- Beyond resorption: targeting osteoclast fusion and polarization to restore balanced bone remodeling.Frontiers in pharmacology · 2026Review
- The Non-receptor Tyrosine Kinase Pyk2 in Brain Function and Neurological and Psychiatric Diseases.Frontiers in synaptic neuroscience · 2021Review
- Pyk2 deficiency enhances bone mass during midpalatal suture expansion.Orthodontics & craniofacial research · 2020Article
- A Pyk2 inhibitor incorporated into a PEGDA-gelatin hydrogel promotes osteoblast activity and mineral deposition.Biomedical materials (Bristol, England) · 2019Article
- Non-canonical Wnt signals regulate cytoskeletal remodeling in osteoclasts.Cellular and molecular life sciences : CMLS · 2018Review
- The HIV co-receptor CCR5 regulates osteoclast function.Nature communications · 2017Article
- Dynamics of the sealing zone in cultured osteoclasts.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Dynamin2 controls Rap1 activation and integrin clustering in human T lymphocyte adhesion.PloS one · 2017Article
- 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
- C-Mpl Is Expressed on Osteoblasts and Osteoclasts and Is Important in Regulating Skeletal Homeostasis.Journal of cellular biochemistry · 2016Article
- Cytoskeletal rearrangement and Src and PI-3K-dependent Akt activation control GABA(B)R-mediated chemotaxis.Cellular signalling · 2015Article
- The Crosstalk between Osteoclasts and Osteoblasts Is Dependent upon the Composition and Structure of Biphasic Calcium Phosphates.PloS one · 2015Article
- Late stages of the synchronized macrophage fusion in osteoclast formation depend on dynamin.The Biochemical journal · 2014Article
- Dynamin and endocytosis are required for the fusion of osteoclasts and myoblasts.The Journal of cell biology · 2014Article
- Tyrosine 402 phosphorylation of Pyk2 is involved in ionomycin-induced neurotransmitter release.PloS one · 2014Article
- Microtubule dynamic instability controls podosome patterning in osteoclasts through EB1, cortactin, and Src.Molecular and cellular biology · 2014Article
- Osteoblast differentiation and migration are regulated by dynamin GTPase activity.The international journal of biochemistry & cell biology · 2014Article
- Podosome organization drives osteoclast-mediated bone resorption.Cell adhesion & migration · 2014Review
- Role of dynamin 2 in the disassembly of focal adhesions.Journal of molecular medicine (Berlin, Germany) · 2013Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Signaling via the Pyk2-Src-Cbl complex downstream of integrins contributes to the assembly, organization, and dynamics of podosomes, which are the transient adhesion complexes of highly motile cells such as osteoclasts and dendritic cells. We previously demonstrated that the GTPase dynamin is associated with podosomes, regulates actin flux in podosomes, and promotes bone resorption by osteoclasts. We report here that dynamin associates with Pyk2, independent of dynamin's GTPase activity, and reduces Pyk2 Y402 phosphorylation in a GTPase-dependent manner, leading to decreased Src binding to Pyk2. Overexpressing dynamin decreased the macrophage colony-stimulating factor- and adhesion-induced phosphorylation of Pyk2 in osteoclastlike cells, suggesting that dynamin is likely to regulate Src-Pyk2 binding downstream of integrins and growth factor receptors with important cellular consequences. Furthermore, catalytically active Src promotes dynamin-Pyk2 association, and mutating specific Src-phosphorylated tyrosine residues in dynamin blunts the dynamin-induced decrease in Pyk2 phosphorylation. Thus, since Src binds to Pyk2 through its interaction with phospho-Y402, our results suggest that Src activates a negative-feedback loop downstream of integrin engagement and other stimuli by promoting both the binding of dynamin to Pyk2-containing complexes and the dynamin-dependent decrease in Pyk2 Y402 phosphorylation, ultimately leading to the dissociation of Src from Pyk2.
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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.