Dr. Swank has been a member of the RPI faculty since 2005. He heads a dynamic, multidisciplinary laboratory of students, staff, and post-docs. His laboratory investigates how muscle is able to power an amazingly wide variety of locomotory tasks and modulate heart function. Research focuses in the lab include determining how variation between muscle fiber types (e.g. slow versus fast-contracting fibers) is generated, the mechanisms behind muscle mechanical properties such as stretch activation, and muscle diseases such as hypertrophic cardiomyopathy. An integrative approach is taken, starting with muscle genes and moving up in scale to protein expression and function, muscle mechanics, and whole organism studies. His research team primarily uses Drosophila for their studies, due to Drosophila's ease of genetic manipulation and mechanically testable muscles. However, we have recently started using mammalian muscle types to gain further insights.
Dr Swank's lab has primarily focused on the role of myosin, the molecular motor that powers muscle contraction, in modulating muscle mechanical properties. 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 rate and actin sliding velocity. 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 changes in locomotion, such as flight ability. Besides myosin, the laboratory also investigates the function of other muscle proteins such as muscle LIM protein (MLP), actin and troponin C.
The lab investigates mechanisms behind several muscle and heart diseases such as familial hypertrophic cardiomyopathy (HCM) and distal arthrogryposis. FHC is an inherited genetic disease that is the leading cause of sudden cardiac arrest among young adults. The lab creates transgenic Drosophila models of these diseases and perform experiments to determine how these disease states alter the mechanical function of muscle and tp provide insights into possible treatments.
For more information about Dr. Swank's research and team members, visit the Swank laboratory web site: http://homepages.rpi.edu/~swankd/
B.S. University of Rochester, 1990, Biology
Ph.D., University of Pennsylvania, 1995, Physiology
Postdoctoral Fellow, San Diego State University, 2000, Drosophila Genetics
Postdoctoral Fellow, University of Vermont, 2005, Muscle Mechanics
- Our most recent work is listed below. A full publication list is available at: http://homepages.rpi.edu/~swankd/publication.html
- Kronert, W.A., K.M. BellG, M.C. Viswanathan, G.C. Melkani, A.S. Trujillo, A. Huang, A. Melkani, A. Cammarato, D.M. Swank, and S.I. Bernstein (2018) Prolonged cross-bridge binding triggers muscle dysfunction in a Drosophila model of myosin-based hypertrophic cardiomyopathy. elife. 7: e38064. (Comment in: Too much of a good thing. elife, 2018).
- Glasheen, B.M., S. Ramanath, M. Patel, D. Sheppard, J.T. Puthawala, L.A. Riley, and D.M. Swank (2018) Five alternative myosin converter domains influence Drosophila muscle power, stretch activation, cross-bridge kinetics and flight. Biophysical Journal. 114:1142-1152.
- Glasheen, B.M., C.C. Eldred, L.C. Sullivan, C. Zhao, M.K. Reedy, R.J. Edwards, D.M. Swank (2017) Stretch activation properties of Drosophila and Lethocerus indirect flight muscle suggest similar calcium dependent mechanisms. Am. J. Physiol. Cell Physiol. 313(6):C621-C631.
- Suggs J.A., Melkani G.C., Glasheen B.M., Detor M.M., Melkani A., Marsan N.P., Swank D.M., Bernstein S.I. (2017) A Drosophila model of dominant inclusion body myopathy type 3 shows diminished myosin kinetics that reduce muscle power and yield myofibrillar defects. Disease Models & Mechanisms 10(6):761-771.
- Zhao C., Swank D.M. (2017) The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type. American Journal of Physiology: Cell Physiology 312(2):C111-C118.
- Achal M., Trujillo A.S., Melkani G.C., Farman G.P., Ocorr K., Viswanathan M.C., Kaushik G., Newhard C.S., Glasheen B.M., Melkani A., Suggs J.A., Moore J.R., Swank D.M., Bodmer R., Cammarato A., and Bernstein S.I. (2016) A Restrictive Cardiomyopathy Mutation in an Invariant Proline at the Myosin Head/Rod Junction Enhances Head Flexibility and Function, Yielding Muscle Defects in Drosophila. Journal of Molecular Biology 428(11):2446-61.
- Koppes R.A., Swank D.M., Corr D.T. (2015) A new experimental model for force enhancement: steady-state and transient observations of the Drosophila jump muscle. American Journal of Physiology: Cell Physiology 309(8):C551-7.
- Eldred, C.C., A. Katzemich, M. Patel, B. Bullard and D.M. Swank (2014) The roles of troponin C isoforms in the mechanical function of Drosophila indirect flight muscle. Journal of Muscle Research and Cell Motility 35(3-4):211-23.
- Koppes R.A., D.M. Swank, and D.T. Corr (2014) A new experimental model to study force depression: the Drosophila jump muscle. Journal of Applied Physiology 116: 1543-1550.
- Eldred, C.C., N. Naber, R. Cooke, E. Pate, and D. M. Swank (2013) Conformational changes at the nucleotide site in the presence of bound ADP do not set the velocity of fast Drosophila myosins. Journal of Muscle Research and Cell Motility: 34:35-42.
- Zhao, C. and D.M. Swank (2013) An embryonic myosin isoform enables stretch activation and cyclical power in Drosophila jump muscle. Biophysical Journal 104:2662-2670.
- Wang, Q., C.S. Newhard, S. Ramanath, D. Sheppard, and D.M. Swank (2013) An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight. Journal of Experimental Biology 217:290-298.
- Swank, D.M. (2012) Mechanical analysis of Drosophila indirect flight and jump muscles. Methods 56:69-77.
- Wang, Q., C. Zhao and D.M. Swank (2011) Calcium and stretch-activation modulate power generation in Drosophila flight muscle. Biophyical Journal 101: 2207-2213.
- 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 101: 1114-1122.
- 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. Eldred, 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.
- 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 95:5228-5237.
- 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.
- Hao, Y., M. S. Miller, D. M. Swank, H. Liu, S. I. Bernstein, D. W. Maughan, G. H. Pollack (2006) Passive stiffness in Drosophila indirect flight muscle is reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution. Biophysical J. 103:17543-17547.
- 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.
- 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., 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.