Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):3088-92.

Transactivation and transformation by Myb are negatively regulated by a leucine-zipper structure.

Kanei-Ishii C, MacMillan EM, Nomura T, Sarai A, Ramsay RG, Aimoto S, Ishii S, Gonda TJ.

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Tsukuba Life Science Center, Institute of Physical and Chemical Research (RIKEN), Ibaraki, Japan.

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.

PMID:: 1557416; [PubMed - indexed for MEDLINE]
PMCID:: PMC48809

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Transactivation and transformation by Myb are negatively regulated by a leucine-...
Transactivation and transformation by Myb are negatively regulated by a leucine-zipper structure.
Proc Natl Acad Sci U S A. 1992 Apr 1 ;89(7):3088-92.

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