Josiah Meigs Professor
Ph.D., 1980
Johns Hopkins University

RESEARCH

We are interested in the cellular machinery responsible for maintenance of cell shape and production of force for cell movements. It is now well established that actin and myosin play primary roles in single cell movements such as locomotion, chemotaxis, phagocytosis, and cytokinesis. Regulation of the structure and activity of these molecules is required to achieve proper spatial and temporal regulation that is needed to produce coordinated movements. Our primary focus is on the role of actin binding proteins as regulators of the eucaryotic cytoskeleton. The assembly and interactions of these proteins in vitro are investigated using optical approaches including fluorescence spectroscopy and classical light scattering. Molecular cloning, expression, and mutagenesis are being employed to dissect the interactions among cytoskeletal proteins in vitro and in living cells. In addition, homologous recombination is employed to create cell lines with specific defects in single genes in order to test the roles of these proteins in cell structure and movement. To unravel redundant networks among cytoskeletal proteins, cells with defects in multiple proteins are also being generated. Expression of altered forms of the molecules in wild type and mutant strains allows investigation of the mechanisms directing subcellular localization, and tests of the significance of specific molecular interactions for cell function.

Slime mold

We have recently begun investigations of the biochemistry, genetics, and physiology of Hirano Bodies, aberrant actin filament containing structures observed in association with a number of conditions including Alzheimer�s disease, Parkinson�s disease, Amyotrophic Lateral Sclerosis, diabetes, and chronic alcoholism. Methods to induce formation of Hirano bodies in Dictyostelium and cultured mammalian cells have been developed. Biochemical purification of Hirano bodies is being undertaken in order to identify all major protein constituents of Hirano bodies. The mechanisms of formation and fate of Hirano bodies are also under investigation. Development of stable cell lines will allow studies of the physiological effects of Hirano bodies on cell function.

CONTACT INFORMATION

(706) 542-3338, fechheim@cb.uga.edu

SEE ALSO

Biomedical & Health Sciences Institute Press Release: "Alzheimer's, Other Diseases, May Benefit from First Live Studies of Key Cell Structures".

OF NOTE

• General Sandy Beaver Award for Excellence in Teaching from the Franklin College, 1992
• General Sandy Beaver Teaching Professor of the Franklin College. 2001- present.
• Student Government Association Outstanding Professor Award. 2001

SUPPORT STAFF

	Griffin

NAME		POSITION		E-MAIL
Paul Griffin		Grad Student		paulgrif@uga.edu

REPRESENTATIVE PUBLICATIONS

Ha, Sang Deuk, R. Furukawa, and M. Fechheimer. A mouse model for Hirano bodies. manuscript in preparation.

Ha, Sang Deuk, R. Furukawa, and M. Fechheimer. 2008. Association of the Carboxy terminal domain of the amyloid precursor protein with Hirano bodies, manuscript in revision.

Kim, D.-H., R. C. Davis, R. Furukawa, and M. Fechheimer. 2008. Degradation of Hirano Bodies by Autophagy, manuscript in revision.

Davis, R. C., Furukawa, R., and M. Fechheimer, 2008. A cell culture model for investigation of Hirano bodies. Acta Neuropathol. 2008 Feb;115(2):205-17

Furukawa, R., and M. Fechheimer. 2006. Characterization of cross-linked actin filament gels and bundles using birefringence and polarized light scattering. Methods Mol Biol. 346:407-21.

Pikzack, C., J. Prassler, R. Furukawa, M. Fechheimer, and F. Rivero. 2005. Role of Calcium-dependent actin-bundling proteins: characterization of Dictyostelium mutants lacking fimbrin and the 34 kDa protein. Cell Motility and the Cytoskeleton 62, 210-231.

Stich, R. W., G. A. Olah, K. A. Brayton, W. C. Brown, M. Fechheimer, K. Green-Church, S. Jittapalapong, K. M. Kocan, T. C. McGuire, F. R. Rurangirwa, and G. H. Palmer. 2004. Infection and Immunity 72, 7257-7264.

Maselli, A., R. Furukawa, S. A. M. Thomson, R. C. Davis, and M. Fechheimer. 2003. Formation of Hirano Bodies Induced by Expression of an Actin Cross-linking Protein With a Gain of Function Mutation. Eucaryotic Cell 2, 778-787.

Furukawa, R., A. Maselli, S. A. M. Thomson, R. W. L. Lim, J. Stokes, and M. Fechheimer. 2003. Calcium Regulation of Actin Cross-linking Is Important for Function of the Actin Cytoskeleton in Dictyostelium, Journal of Cell Science 116, 187-196.

Maselli, A. G., R. Davis, R. Furukawa, and M. Fechheimer. 2002. Formation of Hirano Bodies in Dictyostelium and Mammalian Cells Induced by Expression of a Modified form of an Actin Cross-linking Protein. J. Cell Science 115, 1939-1952.

Fechheimer M, Furukawa R, Maselli A, Davis RC. 2002. Hirano bodies in health and disease. Trends Mol Med. 8(12):590-1.

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