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, and the mechanisms behind muscle mechanical properties such as stretch activation and force enhancement. 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. This comprehensive approach is possible by exploiting the unique genetic properties and transgenic techniques available for Drosophila.
We have 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 laboratory also investigates mechanisms behind muscle disease states such as familial hypertrophic cardiomyopathy (FHC) and distal arthrogryposis. FHC is an inherited genetic disease that is the leading cause of sudden cardiac arrest among young adults. We create transgenic Drosophila models of these disease and perform experiments to determine how these disease states alter the mechanical function of muscle.
Dr. Swank teaching responsibilities include Human Physiology and various graduate level courses.
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
- 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.