| First Author | De Valck D | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 238 |
| Issue | 2 | Pages | 590-4 |
| PubMed ID | 9299557 | Mgi Jnum | J:186078 |
| Mgi Id | MGI:5430903 | Doi | 10.1006/bbrc.1997.7343 |
| Citation | De Valck D, et al. (1997) A20 inhibits NF-kappaB activation independently of binding to 14-3-3 proteins. Biochem Biophys Res Commun 238(2):590-4 |
| abstractText | The A20 protein, which belongs to a class of Cys2/Cys2 zinc finger proteins, has been characterized as an inhibitor of NF-kappaB activation. In order to clarify its molecular mechanism of action, the yeast two-hybrid system was used to screen for interacting proteins. We report that different isoforms of 14-3-3 proteins, viz. eta and zeta, are able to bind A20, involving the 14-3-3-binding motif RSKSDP located between zinc fingers 3 and 4. However, A20 mutants that no longer associated with 14-3-3 proteins could still fully inhibit NF-kappaB activation induced by tumor necrosis factor, interleukin-1beta or phorbol 12-myristate 13-acetate, thus excluding a crucial role for 14-3-3 interaction in this A20 function. |
