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| Name |
Korn, Edward D. |
| Location
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National Institutes of Health |
| Primary Field
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Biochemistry |
 Election Citation
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Korn obtained early evidence for actin filaments in nonmuscle cells and for their association with the plasma membrane; elucidated the regulatory roles of actin-binding proteins and ATP hydrolysis in actin polymerization; and discovered single-headed, non-filamentous myosins and the regulation of nonmuscle myosins by heavy chain phosphorylation. |
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Research Interests
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Current research focuses on the structural basis of the biochemical and biological properties of non-muscle myosin II, more specifically, the effects of specific mutations on the biochemical properties, as determined in vitro, and the biological functions in vivo of myosin II of Dictyostelium discoideum and the correlation between the biochemistry and biology. The principal biochemical properties studied are the actinactivated MgATPase activity and the ability of myosin to translocate actin filaments. The biological functions of Dictyostelium discoideum that require myosin II are cytokinesis of cells growing in suspension culture, patching and capping of surface receptors and development and differentiation progressing from the ameboid stage to fully developed fruiting bodies. We are also interested in the mechanism by which myosin II translocates to the cleavage furrow of dividing cells. Studies on the structural basis of regulation of the actin-activated MgATPase activity of myosin II from Acanthamoeba castellanii by phosphorylation at the tip of the tail of the heavy chain continue and, recently, we have begun to study the formation and function of tyrosine-phosphorylated actin in Dictyostelium discoideum. |
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