| First Author | Fang D | Year | 2001 |
| Journal | Nat Immunol | Volume | 2 |
| Issue | 9 | Pages | 870-5 |
| PubMed ID | 11526404 | Mgi Jnum | J:125680 |
| Mgi Id | MGI:3759395 | Doi | 10.1038/ni0901-870 |
| Citation | Fang D, et al. (2001) Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells. Nat Immunol 2(9):870-5 |
| abstractText | Cbl-b, a ring-type E3 ubiquitin protein ligase, is implicated in setting the threshold of T lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (PI3K) was identified as a substrate for Cbl-b. We have shown that Cbl-b negatively regulated p85 in a proteolysis-independent manner. Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor zeta through its E3 ubiquitin ligase activity. The enhanced activation of Cbl-b(-/-) T cells was suppressed by the inhibition of PI3K. The results suggest a proteolysis-independent function for Cbl-b in the modification of protein recruitment. |
