Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization.

Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Research Abstract Details 

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Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Abstract Text:

L Zhang,J D'Costa,T Kummalue,C I Civin,A D Friedman,

In the core binding factor (CBF)beta-smooth muscle myosin heavy chain (SMMHC) acute myeloid leukemia (AML) oncoprotein, CBFbeta lies N-terminal to the alpha-helical rod domain of SMMHC. Deletion of the SMMHC assembly competence domain (ACD), conserved among skeletal, smooth and nonmuscle myosins, prevents multimerization, inhibition of CBF and inhibition of cell proliferation. To define the amino acids critical for ACD function, three outer surface residues of ACD helices A-D, the subsequent helices E-H or the more N-terminal X or Z helices were now mutated. Variants were assessed for multimerization in low ionic strength in vitro and for nuclear localization as a measure of in vivo multimerization. Mutation of individual helices C-H reduced multimerization, with alteration of the outer surface of helices D or E having the greatest effect. The ability of these SMMHC variants to slow murine myeloid progenitor proliferation largely paralleled their effects on multimerization. Divergence at the boundaries of the ACD may reflect quantitative differences between in vitro and in vivo filament assembly. Each helix mutant retained the ability to bind the mSin3A corepressor. Agents interacting with the outer surface of the CBFbeta-SMMHC ACD that prevent multimerization may be effective as novel therapeutics in AML.

Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Publishing Authors By Initials

L Zhang,J D'Costa,T Kummalue,CI Civin,AD Friedman,

For similar proteins: mutant proteins: mutant chimeric proteins: oncogene proteins, fusion research abstracts see: proteins: mutant proteins: mutant chimeric proteins: oncogene proteins, fusion research

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Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Oncogene

VOLUME: 25

Page Numbers: 7289-96

Journal Abbreviation: Oncogene

ISSN: 0950-9232

DAY: 12

MONTH: 06

YEAR: 2006

Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Information

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LANGUAGE: eng

NlmUniqueID: 8711562

Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Keywords Mesh Terms:

KEYWORDS: Oncogene Proteins, Fusion

MESH TERMS: metabolism

Chemical & Substance for Abstract: Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization. Information

Substance Name: Oncogene Proteins, Fusion

Registry Number: 0

Grant and Affiliation Information for Identification of a region on the outer surface of the CBFbeta-SMMHC myeloid oncoprotein assembly competence domain critical for multimerization.

AFFILIATION: Divisions of Pediatric Oncology and Immunology and Hematopoiesis, Johns Hopkins University, Baltimore, MD 21231, USA.

Country: England

AGENCY: United States NCI

GRANT: CA098805

ACRONYM: CA

MEDLINETA: Oncogene

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