MARCUS FECHHEIMER
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.
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.
Slime mold
| 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". |
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| Paul Griffin | |
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| Sang-Deuk Ha | |
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REPRESENTATIVE PUBLICATIONS
Furukawa, R., and M. Fechheimer. (1996). Role of the Dictyostelium 30 kDa protein in actin bundle formation. Biochemistry. 35, 7224-7232.Rivero, F., R. Furukawa, A.A. Noegel, and M. Fechheimer. (1996). Dictyostelium discoideum cells lacking the 34,000 dalton actin binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy. J. Cell Biol. 135, 965-980.
Fisher, P.R., A. A. Noegel, M. Fechheimer, F. Rivero, J. Prassler, and G. Gerisch. 1997. Photosensory and thermosensory responses in Dictyostelium slugs are specifically impaired by absence of the F-actin cross-linking gelation factor (ABP-120). Current Biology 7, 889-892.
Stich, R.W., K.M. Kocan, R.T. Damian, and M. Fechheimer. 1997. Inclusion appendages associated with the intraerythrocytic rickettsial parasite Anaplasma marginale are composed of bundled actin filaments. Protoplasma 199, 93-98.
Furukawa, R., and M. Fechheimer. 1997. The Structure, Function and Assembly of Actin Filament Bundles. International Reviews of Cytology 175, 29-90.
Narcisi, E.M., C.V.C. Glover, and M. Fechheimer. 1998. Fibrillarin, A Conserved pre-Ribosomal RNA Processor of Giardia., J. Euk. Microbiol. 45, 105-111.
Lim, R.W.L., R. Furukawa, S. Eagle, R.C. Cartwright, and M. Fechheimer. 1999. Three distinct F-actin binding sites in the Dictyostelium discoideum 34,000 dalton Actin Bundling Protein. Biochemistry, 38, 800-812.
Rivero, F., R. Furukawa, M. Fechheimer, and A.A. Noegel. Three actin cross-linking proteins, the 34 kDa actin-bundling protein, a -actinin, and ABP-120, have both unique and redundant roles in growth and development of Dictyostelium. J. Cell Science 112, 2737-2751.
Lim, R. W. L., R. Furukawa, and Fechheimer. 1999. Evidence of Intramolecular Regulation of the Dictyostelium discoideum 34,000 dalton F-actin Bundling Protein. Biochemistry 38, 16323-16332.
Ponte, E., F. Rivero, M. Fechheimer, A. Noegel, and S. Bozzaro. 2000. Severe Developmental Defects in Dictyostelium Null Mutants for Actin Binding Proteins. Mechanisms of Development 91, 153-161
Furukawa, R.T.M. Jinks, T. Tishgaren, M. Mazzawi, D. R. Morris, and M. Fechheimer. 2001. Biochimica et Biophysica Acta. 1527, 130-140.
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.
Meagher, R.B., and M. Fechheimer. 2002. The Arabidopsis Cytoskeletal Genome in "The Arabidopsis Book", ed. by C. Sommerville. In press. 67 pages.
Furukawa, R., A. Maselli, S.A.M. Thomson, R.W.L. Lim, J. Stokes, and M. Fechheimer. 2002. Calcium Regulation of Actin Cross-linking Is Important for Function of the Actin Cytoskeleton in Dictyostelium, submitted to J. Cell Science.
Maselli, A., S.A.M. Thomson, R. Davis, R. Furukawa, and M. Fechheimer. Formation of Hirano Bodies Induced by Expression of a Modified Form of an Actin Cross-linking Protein With Point Mutations that Activate Actin Binding , manuscript submitted.