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  • Prof.  andras Muhlrad
Born 1932, Budapest;
Ph.D. 1959, Eotvos Lorand Univ. (Budapest);
Assoc. Prof. (HU) 1974;
Prof. 1981;
Emeritus 2000
Membership in professional societies.
Biophysical Society
American Society of Cell Biology 
Research Interests &Projects:
The study of the main cytoskeletal proteins, actin and myosin, has been going on in my laboratory for a long time, which was resulted more than 130 publications. These proteins are present in all eukaryotic cells and have a major role in the formation of the cytoskeleton and in biological motility. In the last couple of years we concentrated on studying the structure of the actin filament and the effect of actin binding proteins, such as tropomyosin and cofilin, on filament (actin polymer) structure and function. Our studies on cofilin (ubiquitous actin-binding protein regulating actin dynamics) effect on actin structure will be continued. In the future we shall investigate the cofilin induced changes in the molecular structure of actin monomer.
Another connected area of our research is the study of the formation and dissociation of actin filaments. These processes constantly going on in the cell and their dynamic nature have a great significance in cell physiology. Polycations were found to accelerate greatly actin polymerization, however, the mechanism and the details of this process remained unknown. We study the effect of nucleotides, pH, temperature, monovalent and divalent cations on the polycation polymerization of the various forms of actin monomers, such as CaATP-G-actin, MgATP-G-actin and MgADP-G-actin. Actin polymerization starts with nuclei formation, which is followed by elongation of the filament. The effect of polycations on the kinetics of both steps will be investigated separately. Polycations also bundles actin filaments. These bundles have important function in the cell, i.e. they form microvilli and stress fibers, which constitute the skeleton of the cell. The kinetics of the polycation induced bundle formation and the connection between bundling and polymerization of actin is also studied. Polylysine is used as polycation model and its effect is compared with naturally occurring polycations, such as lysozyme and basic myelin protein.
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