Transactivation and transformation by Myb are negatively regulated by a leucine-zipper structure.
Abstract
The negative regulatory domain of the c-myb protooncogene product (c-Myb) normally represses transcriptional activation by c-Myb. We show here that a leucine-zipper structure is a component of the negative regulatory domain, because its disruption markedly increases both the transactivating and transforming capacities of c-Myb. We also demonstrate that this leucine-zipper structure can interact with cellular proteins. Our results suggest that an inhibitor that suppresses transactivation binds to c-Myb through the leucine zipper and that c-Myb can be oncogenically activated by missense mutation.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- April 1992
- DOI:
- 10.1073/pnas.89.7.3088
- Bibcode:
- 1992PNAS...89.3088K