| Literature DB >> 1557416 |
C Kanei-Ishii1, E M MacMillan, T Nomura, A Sarai, R G Ramsay, S Aimoto, S Ishii, T J Gonda.
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.Entities:
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Year: 1992 PMID： 1557416 PMCID： PMC48809 DOI： 10.1073/pnas.89.7.3088
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205