erk and pi-3 kinase are necessary for collagen binding in corneal epithelia
| PAG Title | erk and pi-3 kinase are necessary for collagen binding in corneal epithelia |
| PAG ID | WAG001020 |
| Type | P |
| Source Link |  BioCarta |
| Publication Reference | NA |
| PAG Description | Activation of the MAPK kise pathway has been identified as a mechanism that integrins use to regulate gene expression leading to cell shape changes during cell spreading or migration Epithelial cells respond to extracellular matrix (ECM) cause integrin-mediated FAK phosphorylation that in turn phosphorylates the surrounding proteins (paxillin, Fyn/shc, and src) and leads to sigl amplification. FAK also binds PI-3 kise and is upstream of the MAP kise pathway. When MAPkise or PI-3 kise was inhibited, actin reorganization was blocked. Src phosphorylates p190RhoGAP, ictivating its GAP function that may allow RhoGTP to stay active longer, promoting further sigl amplification. Activated RhoGTP binds to downstream kises such as Rho-associated coiled coil-containing protein kise (p160ROCK) and p140 diaphanous (p140Dia) to increase actin polymerization and contraction. Actin reorganization assists integrin clustering, allowing more ECM binding that increase FAK phosphorylation and other sigl transduction events. |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 4,183 |
| Information Content | Rich |
| Other IDs | |
| Base PAG ID | WAG001020 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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