ArticleProceedings of the National Academy of Sciences of the United States of America2004
CrkII regulates focal adhesion kinase activation by making a complex with Crk-associated substrate, p130Cas.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- CrkII/Abl phosphorylation cascade is critical for NLRC4 inflammasome activity and is blocked by Pseudomonas aeruginosa ExoT.Nature communications · 2022Article
- Synergistic phase separation of two pathways promotes integrin clustering and nascent adhesion formation.eLife · 2022Article
- Proteomic analysis of desmosomes reveals novel components required for epidermal integrity.Molecular biology of the cell · 2020Article
- Regulating Axonal Responses to Injury: The Intersection between Signaling Pathways Involved in Axon Myelination and The Inhibition of Axon Regeneration.Frontiers in molecular neuroscience · 2016Review
- The matricellular protein CCN1 mediates neutrophil efferocytosis in cutaneous wound healing.Nature communications · 2015Article
- Interaction of crk with Myosin-1c participates in fibronectin-induced cell spreading.International journal of biological sciences · 2013Article
- SIRT3 functions in the nucleus in the control of stress-related gene expression.Molecular and cellular biology · 2012Article
- Crk adaptor proteins act as key signaling integrators for breast tumorigenesis.Breast cancer research : BCR · 2012Article
- Models of crk adaptor proteins in cancer.Genes & cancer · 2012Article
- Proteins that bind the Src homology 3 domain of CrkI have distinct roles in Crk transformation.Oncogene · 2010Article
- Integrin signalling adaptors: not only figurants in the cancer story.Nature reviews. Cancer · 2010Review
- ZF21 protein regulates cell adhesion and motility.The Journal of biological chemistry · 2010Article
- CAS proteins in normal and pathological cell growth control.Cellular and molecular life sciences : CMLS · 2010Review
- Crk and CrkL adaptor proteins: networks for physiological and pathological signaling.Cell communication and signaling : CCS · 2009Article
- Regulation of focal adhesion turnover by ErbB signalling in invasive breast cancer cells.British journal of cancer · 2009Article
- FERM control of FAK function: implications for cancer therapy.Cell cycle (Georgetown, Tex.) · 2008Review
- Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis.Journal of cell science · 2008Article
- Extracellular matrix and its role in spermatogenesis.Advances in experimental medicine and biology · 2008Review
- Conditional deletion of focal adhesion kinase leads to defects in ventricular septation and outflow tract alignment.Molecular and cellular biology · 2007Article
- Interaction of CagA with Crk plays an important role in Helicobacter pylori-induced loss of gastric epithelial cell adhesion.The Journal of experimental medicine · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CrkII is an adaptor protein possessing oncogenic potential despite the lack of an enzymatic domain. We investigated here the physiological functions of CrkII by studying its ability to induce anchorage-independent cell growth. We found that inhibition or null mutation of focal adhesion kinase (FAK) blocked the anchorage-independent growth induced by CrkII overexpression, indicating that FAK is a critical determinant of the transforming activity of CrkII. CrkII overexpression enhanced the autophosphorylation of FAK at Tyr-397 and tyrosine phosphorylation of p130(Cas) (Crk-associated substrate, Cas) upon stimulation of integrin by fibronectin. Moreover, the constitutive phosphorylation of FAK and Cas was observed in CrkII-overexpressing cells, even when they were in the suspended condition, consistent with the ability of CrkII to induce anchorage-independent growth. Using Cas-deficient cells, we showed Cas function to be essential for both the CrkII-induced phosphorylation of FAK (Tyr-397) and anchorage-independent cell growth. The CrkII-induced FAK autophosphorylation depended upon CrkII-Cas complex formation. Furthermore, we showed that CrkII knockdown resulted in defects in integrin-mediated events, such as cell spreading, haptotactic migration, and FAK autophosphorylation. The integrin-mediated FAK autophosphorylation was also reduced in Cas-deficient cells. These results suggest that the CrkII-Cas complex functions in integrin-mediated FAK activation signaling. Our findings show the importance of CrkII in integrin-mediated events, acting upstream of FAK to affect the activation of this kinase, which appears to have a central role in this pathway.
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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.