| First Author | Nelms K | Year | 1998 |
| Journal | Immunity | Volume | 9 |
| Issue | 1 | Pages | 13-24 |
| PubMed ID | 9697832 | Mgi Jnum | J:43960 |
| Mgi Id | MGI:1099197 | Doi | 10.1016/s1074-7613(00)80584-1 |
| Citation | Nelms K, et al. (1998) FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation. Immunity 9(1):13-24 |
| abstractText | The human IL-4 receptor contains a sequence (the 14R motif) centered on Y497 that, when phosphorylated, interacts with phosphotyrosine-binding (PTB) domain proteins. Here, we describe a PTB domain protein, FRIP, that is phosphorylated in response to cytokine stimulation. FRIP is related to the rasGAP-associated protein p62dok and is bound by the N-terminal SH2 domain of rasGAP. The frip gene maps to the hairless (hr) locus on mouse chromosome 14. hr/hr mice exhibit lymphadenopathy, and their lymph node T cells proliferate more vigorously to anti-CD3 with IL-4 or IL-2 stimulation than +/hr T cells. FRIP expression is significantly reduced in T cells from hr/hr mice. FRIP may negatively regulate proliferation by acting as an adapter molecule between rasGAP and receptor complexes. |
