Dr. Henry Zot Professor and Chair Cell Physiology hzot@westga.edu 678-839-4016

• Ph.D. University of Miami
• M.S. University of Cincinnati
• B.A . Denison University

My laboratory has had a long-standing interest in how cells move and change shape. Cells that swim by beating flagella or cilia are interesting but I study cells that crawl or contract. These are complex movements that require coordination of events in all parts of the cell. Much of our current work revolves around the cytoskeletal protein, actin, and proteins that interact with actin. We use microscopy and molecular biology as tools to dissect the fundamental mechanisms by which actin contributes to the movement of cell. Our work is relevant to the mechanisms of muscle development and cellular transformation (cancer).

• BIOL 1107 Fundamentals of Biology I

• Zot, H.G. and J.D. Potter (1981) Purification of actin from cardiac muscle. Prep.Biochem. 11:381-395.



• Zot, H.G. and J.D. Potter (1982) A structural role for the Ca²⁺-Mg²⁺ sites of troponin C (TnC) in the regulation of muscle contraction. Preparation and properties of TnC-depleted myofibrils. J. Biol. Chem. 257:7678-7683.



• Zot, H.G., S. Iida, and J.D. Potter (1983) thin filament interaction and Ca²⁺ binding to Tn. Chemica scripta 21:133-136.



• Kerrick, W.G.L., H.G. Zot, P.E. Hoar, and J.D. Potter (1985) Evidence that the Sr²⁺-activation properties of cardiac troponin C are altered when substituted into skinned skeletal muscle fibers J. Biol. Chem. 260:15687-15693.



• Zot, H.G., K. Guth, and J.D. Potter (1986) Fast Skeletal muscle skinned fibers and myofibrils reconstituted with N-terminal fluorescent analogues of troponin C J. Biol. Chem. 261:15883-15890.



• Zot, H.G. and J.D. Potter (1987) Calcium binding and fluorescence measurements of dansylaziridine labeled troponin C in reconstituted thin filaments J. Mus. Res. Cell Motil. 8:428-436.



• Zot, H.G. and D. Puett (1988) Crosslinking of calmodulin to troponin I and myosin light chain kinase with carbodiimides ICSU Short Reports 8:161.



• Zot, H.G. and J.D. Puett (1989) An enzymatically active cross-linked complex of calmodulin and rabbit skeletal muscle myosin light chain kinase. J. Biol. Chem. 264:15552-15555.



• Zot, H.G., R. Aden¹, S. Samy¹, and D. Puett (1990) Association of skeletal muscle myosin light chain kinase with fluorescent adducts of wheat germ calmodulin. J. Biol. Chem. 265:14796-14801.



• Maciver, S.K., H.G. Zot, and T.D. Pollard (1991) Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115:1611-620.



• Kobayashi, T., H.G. Zot, T.D. Pollard, and J.H. Collins (1991) Functional implications of the unusual amino acid sequence for the regulatory light chain of Acanthamoeba myosin-II. J. Muscle Res. Cell Motil. 12:553-559.



• Zot, H.G., Doberstein, S.K., and Pollard, T.D. (1992) Myosin-I moves actin filaments on a phospholipid membrane: implications for membrane targeting. J. Cell Biol. 116:367-376.



• Pollard, T.D., Bhandari, P., Maupin, Wachsstock, D., Weeds, A.G., and Zot, H.G. (1993) Direct visualization by electron microscopy of the weakly-bound intermediates in the actomyosin ATPase cycle. Biophys. J. 64:454-471.



• Parra-Diaz, D., Zot, H.G., Echegoyen, L., and Puett, J.D. (1995) Inhibitory effect of vanadyl on calmodulin-activated skeletal muscle myosin light chain kinase activity BioFactors 6:1-4.



• Zot, H.G. (1995) Phospholipid membrane-associated brush border myosin-I activity. Cell Motil. Cytoskel. 30:26-37.



• Xu, P., Zot, A.S., and Zot, H.G. (1995) Identification of Acan125 as a myosin-I binding protein present with myosin-I on cellular organelles of Acanthamoeba J. Biol. Chem. 270:25316-25319.



• Xu, P., Mitchelhill, Kobe, B., Kemp, B.E., and Zot, H.G. (1997) The myosin-I binding protein, Acan125, binds SH3 and belongs to the superfamily of leucine rich repeat proteins. Proc. Natl. Acad. Sci. USA 94: 3685-3690.



• Lee, W.L., Ostap, E.M., Zot, H.G., and Pollard, T.D. (1999) Hydrodynamic and ligand binding properties of the Acanthamoeba myosin-IA GPA/SH3 domain. J. Biol. Chem. 274:35159-71.



• Zot, H.G. Bhaskara¹ , V., and Liu, L. (2000) Acan125 binding to the SH3 domain of Acanthamoeba myosin-IC. Arch. Biochem. Biophys. 375: 161-164.



• Qian, Y., Baisden, J.M., Zot, H.G., Van Winkle, B., and Flynn, D.C. (2000) The carboxy terminus of AFAP-110 modulates direct interactions with actin filaments and regulates its ability to alter actin filament integrity and induce lamellipodia formation. Ex. Cell Res. 255:102-113



• Baisden, J.M., Qian, Y., Zot, H.G., and Flynn, D.C. (2001) The actin filament-associated protein AFAP-110 is an adapter protein that modulates changes in actin filament integrity. Oncogene 20:6435-47



• Qian, Y., Baisden, J.M., Cherezova, L., Summy, J.M., Guappone-Koay, A., Xianglin, S., Mast¹, T., Pastula¹, J., Zot, H.G., Mazloum, N., Lee, M.Y., and Flynn, D.C. (2002) PKC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments. Mol Biol Cell. 13:2311-22



• Qian, Y., Gatesman, A.S. Baisden, J.M., Zot, H.G., Cherezova, L., Qazi, I., Mazloum, N., Lee, M.Y., Guappone-Koay, A., and Flynn, D.C. (2004) Analysis of the role of the leucine zipper motif in regulating the ability of AFAP-110 to alter actin filament integrity J. Cell. Biochem. 91:602-20