ArticleMolecular and cellular biology2001
Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed, 157 citations in OpenAlex.
- Functional role for Cas cytoplasmic adaptor proteins during cortical axon pathfinding.PLoS genetics · 2025Article
- Current understanding of PEAK family members in regulation of cellular signaling pathways and cancer therapy.Molecular and cellular biochemistry · 2025Review
- Rac1 Suppression by the Focal Adhesion Protein GIT ArfGAP2 and Podocyte Protection.Journal of the American Society of Nephrology : JASN · 2025Article
- FAK-Dependent Cell Motility and Cell Elongation.Cells · 2020Review
- The interaction of p130Cas with PKN3 promotes malignant growth.Molecular oncology · 2019Article
- Therapeutic Potential of Focal Adhesion Kinase Inhibition in Small Cell Lung Cancer.Molecular cancer therapeutics · 2019Article
- Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.Scientific reports · 2017Article
- Dasatinib inhibits actin fiber reorganization and promotes endothelial cell permeability through RhoA-ROCK pathway.Cancer medicine · 2017Article
- In vivo epidermal migration requires focal adhesion targeting of ACF7.Nature communications · 2016Article
- A ligand-independent integrin β1 mechanosensory complex guides spindle orientation.Nature communications · 2016Article
- Novel Role of Src in Priming Pyk2 Phosphorylation.PloS one · 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
- Phosphoproteomic Analysis Identifies Focal Adhesion Kinase 2 (FAK2) as a Potential Therapeutic Target for Tamoxifen Resistance in Breast Cancer.Molecular & cellular proteomics : MCP · 2015Article
- N-Cadherin Induction by ECM Stiffness and FAK Overrides the Spreading Requirement for Proliferation of Vascular Smooth Muscle Cells.Cell reports · 2015Article
- Adaptive responses to dasatinib-treated lung squamous cell cancer cells harboring DDR2 mutations.Cancer research · 2014Article
- p130Cas scaffolds the signalosome to direct adaptor-effector cross talk during Kaposi's sarcoma-associated herpesvirus trafficking in human microvascular dermal endothelial cells.Journal of virology · 2014Article
- A FAK-Cas-Rac-lamellipodin signaling module transduces extracellular matrix stiffness into mechanosensitive cell cycling.Science signaling · 2014Article
- N-WASP-directed actin polymerization activates Cas phosphorylation and lamellipodium spreading.Journal of cell science · 2014Article
- Caspase-8 as a regulator of tumor cell motility.Current molecular medicine · 2014Review
- CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics.Cellular and molecular life sciences : CMLS · 2014Article
21 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Tyrosine phosphorylation of CAS (Crk-associated substrate, p130(Cas)) has been implicated as a key signaling step in integrin control of normal cellular behaviors, including motility, proliferation, and survival. Aberrant CAS tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins, including v-Crk and v-Src, and to tumor growth and metastasis. The CAS substrate domain (SD) contains 15 Tyr-X-X-Pro motifs, which are thought to represent the major tyrosine phosphorylation sites and to function by recruiting downstream signaling effectors, including c-Crk and Nck. CAS makes multiple interactions, direct and indirect, with the tyrosine kinases Src and focal adhesion kinase (FAK), and as a result of this complexity, several plausible models have been proposed for the mechanism of CAS-SD phosphorylation. The objective of this study was to provide experimental tests of these models in order to determine the most likely mechanism(s) of CAS-SD tyrosine phosphorylation by FAK and Src. In vitro kinase assays indicated that FAK has a very poor capacity to phosphorylate CAS-SD, relative to Src. However, FAK expression along with Src was found to be important for achieving high levels of CAS tyrosine phosphorylation in COS-7 cells, as well as recovery of CAS-associated Src activity toward the SD. Structure-functional studies for both FAK and CAS further indicated that FAK plays a major role in regulating CAS-SD phosphorylation by acting as a docking or scaffolding protein to recruit Src to phosphorylate CAS, while a secondary FAK-independent mechanism involves Src directly bound to the CAS Src-binding domain (SBD). Our results do not support models in which FAK either phosphorylates CAS-SD directly or phosphorylates CAS-SBD to promote Src binding to this site.
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