ArticleMolecular biology of the cell2011
Tyrosine phosphorylation within the SH3 domain regulates CAS subcellular localization, cell migration, and invasiveness.
Article in Molecular biology of the cell, 2011. 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, 42 citations in OpenAlex.
- Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase.eLife · 2023Article
- Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023Review
- Emerging Role of Plant-Based Dietary Components in Post-Translational Modifications Associated with Colorectal Cancer.Life (Basel, Switzerland) · 2023Review
- The interaction of p130Cas with PKN3 promotes malignant growth.Molecular oncology · 2019Article
- NEDD9 stimulated MMP9 secretion is required for invadopodia formation in oral squamous cell carcinoma.Oncotarget · 2018Article
- Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.Scientific reports · 2017Article
- Vinculin in cell-cell and cell-matrix adhesions.Cellular and molecular life sciences : CMLS · 2017Review
- The role of focal adhesion anchoring domains of CAS in mechanotransduction.Scientific reports · 2017Article
- The ubiquitin-proteasome system regulates focal adhesions at the leading edge of migrating cells.eLife · 2016Article
- A Kinase-Independent Function of c-Src Mediates p130Cas Phosphorylation at the Serine-639 Site in Pressure Overloaded Myocardium.Journal of cellular biochemistry · 2015Article
- Article
- Review
- PKCα promotes the mesenchymal to amoeboid transition and increases cancer cell invasiveness.BMC cancer · 2015Article
- The clinical implications of Crk-like adaptor protein expression in papillary thyroid microcarcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- A FAK-Cas-Rac-lamellipodin signaling module transduces extracellular matrix stiffness into mechanosensitive cell cycling.Science signaling · 2014Article
- CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics.Cellular and molecular life sciences : CMLS · 2014Article
- Metastasis of aggressive amoeboid sarcoma cells is dependent on Rho/ROCK/MLC signaling.Cell communication and signaling : CCS · 2013Article
- Mechanosensitivity and compositional dynamics of cell-matrix adhesions.EMBO reports · 2013Review
- Invasive cells in animals and plants: searching for LECA machineries in later eukaryotic life.Biology direct · 2013Review
- Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crk-associated substrate (CAS) is a major tyrosine-phosphorylated protein in cells transformed by v-crk and v-src oncogenes and plays an important role in invasiveness of Src-transformed cells. A novel phosphorylation site on CAS, Tyr-12 (Y12) within the ligand-binding hydrophobic pocket of the CAS SH3 domain, was identified and found to be enriched in Src-transformed cells and invasive human carcinoma cells. To study the biological significance of CAS Y12 phosphorylation, phosphomimicking Y12E and nonphosphorylatable Y12F mutants of CAS were studied. The phosphomimicking mutation decreased interaction of the CAS SH3 domain with focal adhesion kinase (FAK) and PTP-PEST and reduced tyrosine phosphorylation of FAK. Live-cell imaging showed that green fluorescent protein-tagged CAS Y12E mutant is, in contrast to wild-type or Y12F CAS, excluded from focal adhesions but retains its localization to podosome-type adhesions. Expression of CAS-Y12F in cas-/- mouse embryonic fibroblasts resulted in hyperphosphorylation of the CAS substrate domain, and this was associated with slower turnover of focal adhesions and decreased cell migration. Moreover, expression of CAS Y12F in Src-transformed cells greatly decreased invasiveness when compared to wild-type CAS expression. These findings reveal an important role of CAS Y12 phosphorylation in the regulation of focal adhesion assembly, cell migration, and invasiveness of Src-transformed cells.
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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.