A p130Castyrosine phosphorylated substrate domain decoy disrupts v-Crk signaling
The adaptor protein p130Cas(Cas) has been shown to be involved in different cellular processes including cell adhesion, migration and transformation. This protein has a substrate domain with up to 15 tyrosines that are potential kinase substrates, able to serve as docking sites for proteins with SH2 or PTB domains. Cas interacts with focal adhesion plaques and is phosphorylated by the tyrosine kinases FAK and Src. A number of effector molecules have been shown to interact with Cas and play a role in its function, including c-crk and v-crk, two adaptor proteins involved in intracellular signaling. Cas function is dependent on tyrosine phosphorylation of its substrate domain, suggesting that tyrosine phosphorylation of Cas in part regulates its control of adhesion and migration. To determine whether the substrate domain alone when tyrosine phosphorylated could signal, we have constructed a chimeric Cas molecule that is phosphorylated independently of upstream signals.
Complete Metadata
| @type | dcat:Dataset |
|---|---|
| accessLevel | public |
| bureauCode |
[
"009:25"
]
|
| contactPoint |
{
"fn": "NIH",
"@type": "vcard:Contact",
"hasEmail": "mailto:info@nih.gov"
}
|
| description | The adaptor protein p130Cas(Cas) has been shown to be involved in different cellular processes including cell adhesion, migration and transformation. This protein has a substrate domain with up to 15 tyrosines that are potential kinase substrates, able to serve as docking sites for proteins with SH2 or PTB domains. Cas interacts with focal adhesion plaques and is phosphorylated by the tyrosine kinases FAK and Src. A number of effector molecules have been shown to interact with Cas and play a role in its function, including c-crk and v-crk, two adaptor proteins involved in intracellular signaling. Cas function is dependent on tyrosine phosphorylation of its substrate domain, suggesting that tyrosine phosphorylation of Cas in part regulates its control of adhesion and migration. To determine whether the substrate domain alone when tyrosine phosphorylated could signal, we have constructed a chimeric Cas molecule that is phosphorylated independently of upstream signals. |
| distribution |
[
{
"@type": "dcat:Distribution",
"title": "Official Government Data Source",
"mediaType": "text/html",
"description": "Visit the original government dataset for complete information, documentation, and data access.",
"downloadURL": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC117778/"
}
]
|
| identifier | https://healthdata.gov/api/views/u9ix-p3mk |
| issued | 2025-07-14 |
| keyword |
[
"cell-adhesion",
"kinase-substrates",
"nih",
"p130cas-protein",
"tyrosine-phosphorylation"
]
|
| landingPage | https://healthdata.gov/d/u9ix-p3mk |
| modified | 2025-09-29 |
| programCode |
[
"009:033"
]
|
| publisher |
{
"name": "National Institutes of Health",
"@type": "org:Organization"
}
|
| theme |
[
"NIH"
]
|
| title | A p130Castyrosine phosphorylated substrate domain decoy disrupts v-Crk signaling |
