| First Author | Sato T | Year | 1995 |
| Journal | Science | Volume | 268 |
| Issue | 5209 | Pages | 411-5 |
| PubMed ID | 7536343 | Mgi Jnum | J:24495 |
| Mgi Id | MGI:72234 | Doi | 10.1126/science.7536343 |
| Citation | Sato T, et al. (1995) FAP-1: a protein tyrosine phosphatase that associates with Fas. Science 268(5209):411-5 |
| abstractText | Fas is a cell surface receptor that controls a poorly understood signal transduction pathway that leads to cell death by means of apoptosis. A protein tyrosine phosphatase, FAP-1, capable of interacting with the cytosolic domain of Fas, was identified. The carboxyl terminal 15 amino acids of Fas are necessary and sufficient for interaction with FAP-1. FAP-1 expression is highest in tissues and cell lines that are relatively resistant to Fas-mediated cytotoxicity. Gene transfer-mediated elevations in FAP-1 partially abolished Fas-induced apoptosis in a T cell line. These findings are consistent with an inhibitory effect of FAP-1 on Fas signal transduction. |
