Structural basis of multimer-mediated mayhem

Cancer Cell
Kajal Sitwala, Jay L Hess

Abstract

Oligomerization of AML1-ETO contributes to leukemogenesis through obscure mechanisms. In this issue of Cancer Cell, Bushweller and colleagues show the crystal structure of the ETO NHR2 domain to be a tetramer. Tetramer formation is important for maturation arrest and self-renewal, and gene expression is altered in the absence of self-association. Loss of oligomer formation disrupts interactions between AML1-ETO and members of the ETO corepressor family, but not other corepressor molecules posited to be important for leukemogenesis. The findings clarify the role of oligomer formation in AML1-ETO function and suggest a possible therapeutic strategy of targeting ETO-corepressor interactions.

References

Oct 3, 2003·Cancer Cell·Mary Ellen MartinJay L Hess
May 8, 2004·Blood·Chi Wai So, Michael L Cleary
May 25, 2004·Oncogene·Bruce A Hug, Mitchell A Lazar
Apr 18, 2006·Cancer Cell·Edison T LiuLance D Miller

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