ArticleMolecular and cellular biology2002
The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.
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Who cites it
179 citing papers in PubMed.
- ERK builds a population of short-lived nascent adhesions that produce persistent edge protrusion and cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Conditional Knockout of Paxillin in Mouse Cortical Pyramidal Neurons Does Not Impair Axon Outgrowth or Corpus Callosum Size.FASEB bioAdvances · 2026Article
- Pathogen hijacks focal adhesion signaling by a T3SS effector CteX.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Paxillin mediates ARP2-dependent actin assembly for spindle migration in mammalian oocyte meiosis.Biology direct · 2026Article
- Paxillin is crucial for thymus and parathyroid development by regulating the architecture of the third pharyngeal pouch endoderm.Cellular and molecular life sciences : CMLS · 2026Article
- ERK builds a population of short-lived nascent adhesions that produce persistent edge protrusion and cell migration.bioRxiv : the preprint server for biology · 2025Article
- Durotaxis is a driver and potential therapeutic target in lung fibrosis and metastatic pancreatic cancer.Nature cell biology · 2025Article
- The influences of ARHGEF9 on myoblasts migration and differentiation.Journal of muscle research and cell motility · 2025Article
- The phosphatase PPM1F, a negative regulator of integrin activity, is essential for embryonic development and controls tumor cell invasion.BMC biology · 2025Article
- Alveolar epithelial paxillin in postnatal lung alveolar development.Biology open · 2025Article
- A comparative analysis of paxillin and Hic-5 proximity interactomes.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Focal Adhesion's Role in Cardiomyocytes Function: From Cardiomyogenesis to Mechanotransduction.Cells · 2024Review
- Paxillin phase separation promotes focal adhesion assembly and integrin signaling.The Journal of cell biology · 2024Article
- Silver Nanoparticles Exposure Impairs Cardiac Development by Suppressing the Focal Adhesion Pathway in Zebrafish.International journal of nanomedicine · 2024Article
- Paxillin regulates liver fibrosis via actin polymerization and ERK activation in hepatic stellate cells.Journal of cell science · 2023Article
- Glaucoma: Novel antifibrotic therapeutics for the trabecular meshwork.European journal of pharmacology · 2023Review
- Paxillin regulates Rab5-mediated vesicle motility through modulating microtubule acetylation.Molecular biology of the cell · 2023Article
- A luciferase fragment complementation assay to detect focal adhesion kinase (FAK) signaling events.Heliyon · 2023Article
- Structure, signal transduction, activation, and inhibition of integrin αIIbβ3.Thrombosis journal · 2023Review
- Delayed cortical development in mice with a neural specific deletion of β1 integrin.Frontiers in neuroscience · 2023Article
119 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
The integrin family of cell adhesion receptors are important for a diverse set of biological responses during development. Although many integrins have been shown to engage a similar set of cytoplasmic effector proteins in vitro, the importance of these proteins in the biological events mediated by different integrin receptors and ligands is uncertain. We have examined the role of one of the best-characterized integrin effectors, the focal adhesion protein paxillin, by disruption of the paxillin gene in mice. Paxillin was found to be critically involved in regulating the development of mesodermally derived structures such as heart and somites. The phenotype of the paxillin(-/-) mice closely resembles that of fibronectin(-/-) mice, suggesting that paxillin is a critical transducer of signals from fibronectin receptors during early development. Paxillin was also found to play a critical role in fibronectin receptor biology ex vivo since cultured paxillin-null fibroblasts display abnormal focal adhesions, reduced cell migration, inefficient localization of focal adhesion kinase (FAK), and reduced fibronectin-induced phosphorylation of FAK, Cas, and mitogen-activated protein kinase. In addition, we found that paxillin-null fibroblasts show some defects in the cortical cytoskeleton and cell spreading on fibronectin, raising the possibility that paxillin could play a role in structures distinct from focal adhesions. Thus, paxillin and fibronectin regulate some common embryonic developmental events, possibly due to paxillin modulation of fibronectin-regulated focal adhesion dynamics and organization of the membrane cytoskeletal structures that regulate cell migration and spreading.
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