Office: Biotechnology Center Rm. 2111
Rensselaer Polytechnic Institute
110 8th Street
Troy, NY 12180
Research Interests
Muscle physiology and motor protein biophysics
Dr. Swank’s laboratory investigates how muscle is designed to perform an amazingly wide variety of tasks including locomotion, pumping blood, and sound production. These studies involve Drosophila, mice, fish, and other organisms likely to reveal novel insights into muscle performance. One aspect of this research is to better understand muscle disease states such as familial hypertrophic cardiomyopathy (FHC). FHC is an inherited genetic disease that is a major cause of sudden death among young adults.
His laboratory’s primary focus is to determine how variation between muscle fiber types (e.g. slow- versus fast-contracting fibers) is generated. An integrative approach is taken, starting with muscle genes such as myosin, and moving up in scale to protein expression and function, muscle mechanics, and whole organism studies. This comprehensive approach is possible by exploiting the unique genetic properties and transgenic techniques available with Drosophila. Drosophila is currently the only system that can be transgenically manipulated to express a specific myosin isoform or mutant myosin in a specific muscle type. The expressed myosin can be isolated from Drosophila to measure single and ensemble biochemical and biophysical molecular properties such as ATPase rates, actin sliding velocity and myosin step size. Laboratory members also measure mechanical properties (e.g. power, velocity and force) of isolated muscle fibers expressing transgenic myosin and relate altered fiber properties to observed changes in locomotion, such as flight ability.
Some of the myosin structural regions Dr. Swank is investigating using Drosophila (e.g. the “converter” region) are hot spots for point mutations that lead to FHC. He is also directly studying the effects of these mutations on cardiac muscle performance using transgenic mouse models of FHC. Besides myosin, the laboratory also investigates the function of other muscle proteins such as muscle LIM protein (MLP), actin, and paramyosin.
Selected Publications
Wang, Q., C. Zhao and D.M. Swank (2011) Calcium and stretch-activation modulate power generation in Drosophila flight muscle. Biophyical Journal (in press).
Ramanath, S., Q. Wang, W. A. Kronert, S. I. Bernstein and D. M. Swank (2011) Disrupting the myosin converter-relay interface impairs Drosophila indirect flight muscle performance. Biophysical Journal (in press).
Clark, K.A., H. Lesage, C. Zhao, M. Beckerle and D. M. Swank (2011) Deletion of Drosophila muscle LIM protein decreases flight muscle stiffness and power generation. Amer. J. Physiol.-Cell 301: C373-C382.
Purcell, T. J., N. Naber, K. Franks-Skiba, A. R. Dunn, C. C. EldredG, C. L. Berger, A. Malnasi-Csizmadia, J. A. Spudich, D. M. Swank, E. Pate, and R. Cooke. (2011). Nucleotide pocket thermodynamics measured by EPR reveal how energy partitioning relates myosin speed to efficiency. J. Mol. Biol. 407:79-91.
Yang, C., C. Kaplan, M. Thatcher and D. M. Swank (2010) The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle. Biophysical Journal 99:1546-1555.
Eldred, C.C. D.R. Simeonov, R.A. Koppes, C. Yang, D.T. Corr and D.M. Swank (2010) The mechanical properties of Drosophila jump muscle expressing wild-type and embryonic myosin isoforms. Biophysical Journal 98:1218-1226.
Miller, M.S., C. M. Dambacher, A. F. Knowles, J. M. Braddock, G. P. Farman, T. C. Irving, D. M. Swank, S. I. Bernstein and David W. Maughan (2009) Alternative S2 hinge regions of the myosin rod affect myofibrillar structure with minor alterations in myosin kinetics. Biophysical Journal 96:4132-4143.
Kronert, W.A., C.A. Dambacher, A.F. Knowles, D.M. Swank and S.I. Bernstein (2008) Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function. J. Mol. Biol. 379:443-456.
Yang, C., S. Ramanath, S. I. Bernstein, D. W. Maughan and D. M. Swank (2008) Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics. Biophysical Journal (in press).
Swank, D.M., V. Vishnudas and D.W. Maughan (2006) An exceptionally fast actomyosin reaction powers insect flight muscle. Proc. Natl. Acad. Sci. 103:17543-17547.
Swank, D.M., J. Braddock, W. Brown, H. Lesage, S.I. Bernstein, and D.W. Maughan (2006) An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics. Biophys. J. 90:2427-2435.
Liu, H., M.S. Miller, D.M. Swank, W.A. Kronert, D.W. Maughan and S.I. Bernstein (2005) Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster. Proc. Natl. Acad. Sci. 102:10522-10527.
Swank, D.M. and J.O. Vigoreaux (2004) The development of the flight and leg muscle. In: Comprehensive Molecular Insect Science, L.I. Gilbert, K. Iantrou and S.S. Gill (eds.) Elsevier Science Ltd. Oxford, UK.
Swank, D.M., A.F. Knowles, W.A. Kronert, J.A. Suggs, G.E. Morrill, M. Nikkoy, G.G. Manipon, and S.I. Bernstein (2003) Variable N-terminal regions of muscle myosin heavy chain modulate ATPase rate and actin sliding velocity. J. Biol. Chem. 278:17475-17482.
Swank, D.M., A.F. Knowles, F. Sarsoza, J.A. Suggs, D.W. Maughan and S.I. Bernstein (2002) The myosin converter domain modulates muscle performance. Nature Cell Biology 4: 312-317.
Swank, D.M., M.L. Bartoo, A.F Knowles, C. Iliffe, S.I. Bernstein, J.E. Molloy, and J.C. Sparrow (2001) Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity. J. Biol. Chem 276: 15117-15124.
Swank, D.M., L. Wells, W.K. Kronert, G. Morrill and S.I Bernstein (2000) Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila. Microscopy Res. and Tech. 50: 430-442.
Swank, D.M. and L.C. Rome (1999) The influence of temperature on power production during swimming I. in vivo length change and stimulation pattern. J. Exp. Biol. 203: 321-331.
Rome, L.C., D.M. Swank and D. Corda (1993) How fish power swimming. Science 261: 340-343.
