ArticleThe Journal of cell biology1997
Induction of apoptosis after expression of PYK2, a tyrosine kinase structurally related to focal adhesion kinase.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 170 citations in OpenAlex.
- Glutamate-induced nuclear translocation of PYK2 in hippocampal neurons, interaction with MBD2, and role in cell death in a model of epilepsy.Cell death & disease · 2026Article
- Generation of BT-Amide, a Bone-Targeted Pyk2 Inhibitor, EffectiveJournal of medicinal chemistry · 2024Article
- PYK2 senses calcium through a disordered dimerization and calmodulin-binding element.Communications biology · 2022Article
- Focal adhesion kinase inhibitors prevent osteoblast mineralization in part due to suppression of Akt-mediated stabilization of osterix.Journal of bone oncology · 2022Article
- Alzheimer risk gene product Pyk2 suppresses tau phosphorylation and phenotypic effects of tauopathy.Molecular neurodegeneration · 2022Article
- The osteocyte as a signaling cell.Physiological reviews · 2022Review
- Proteome profiling of different rat brain regions reveals the modulatory effect of prolonged maternal separation on proteins involved in cell death-related processes.Biological research · 2021Article
- Pyk2 Regulates Human Papillomavirus Replication by Tyrosine Phosphorylation of the E2 Protein.Journal of virology · 2020Article
- Endogenous Control Mechanisms of FAK and PYK2 and Their Relevance to Cancer Development.Cancers · 2018Review
- GLUCOCORTICOID EXCESS IN BONE AND MUSCLE.Clinical reviews in bone and mineral metabolism · 2018Article
- The nonreceptor protein tyrosine kinase Pyk2 promotes the turnover of monocytes at steady state.Journal of leukocyte biology · 2017Article
- Positive and negative regulation by SLP-76/ADAP and Pyk2 of chemokine-stimulated T-lymphocyte adhesion mediated by integrin α4β1.Molecular biology of the cell · 2015Article
- Possible protective effect of membrane lipid rafts against interleukin-1β-mediated anti-proliferative effect in INS-1 cells.PloS one · 2014Article
- Pyk2 regulates megakaryocyte-induced increases in osteoblast number and bone formation.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2013Article
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- Focal adhesion kinase plays a role in osteoblast mechanotransduction in vitro but does not affect load-induced bone formation in vivo.PloS one · 2012Article
- Mefloquine neurotoxicity is mediated by non-receptor tyrosine kinase.Neurotoxicology · 2011Article
- Downregulation of FIP200 induces apoptosis of glioblastoma cells and microvascular endothelial cells by enhancing Pyk2 activity.PloS one · 2011Article
- Recruitment of Pyk2 to SHPS-1 signaling complex is required for IGF-I-dependent mitogenic signaling in vascular smooth muscle cells.Cellular and molecular life sciences : CMLS · 2010Article
- Proline-rich tyrosine kinase 2 regulates hippocampal long-term depression.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Many cells (e.g., epithelial cells) require attachment to the extracellular matrix (ECM) to survive, a phenomenon known as anchorage-dependent cell survival. Disruption of the cell-ECM interactions mediated by the integrin receptors results in apoptosis. Focal adhesion kinase (FAK), a 125-kD protein tyrosine kinase activated by integrin engagement, appears to be involved in mediating cell attachment and survival. Proline-rich tyrosine kinase 2 (PYK2), also known as cellular adhesion kinase beta (CAKbeta) and related adhesion focal tyrosine kinase, is a second member of the FAK subfamily and is activated by an increase in intracellular calcium levels, or treatment with TNFalpha and UV light. However, the function of PYK2 remains largely unknown. In this study, we show that over-expression of PYK2, but not FAK, in rat and mouse fibroblasts leads to apoptotic cell death. Using a series of deletion mutants and chimeric fusion proteins of PYK2/FAK, we determined that the NH2-terminal domain and tyrosine kinase activity of PYK2 were required for the efficient induction of apoptosis. Furthermore, the apoptosis mediated by PYK2 could be suppressed by over-expressing catalytically active v-Src, c-Src, phosphatidylinositol-3-kinase, or Akt/protein kinase B. In addition, it could also be suppressed by overexpressing an ICE or ICE-like proteinase inhibitor, crmA, but not Bcl2. Collectively, our results suggest that PYK2 and FAK, albeit highly homologous in primary structure, appear to have different functions; FAK is required for cell survival, whereas PYK2 induces apoptosis in fibroblasts.
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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 Socratic graph.