Professor, Biological Sciences
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. HCM 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
- Heart Disease
- Muscle Disease
- Cardiac Physiology
- Muscle Physiology
- Motor Proteins
- Drosophila Genetics
- Our most recent work is listed below. A full publication list is available at: http://homepages.rpi.edu/~swankd/publication.html
- Bell, K.M., A. Huang, W.A. Kronert, S.I. Bernstein and D.M. Swank (2020) Prolonged myosin binding is the mechanism behind increased Muscle Stiffness in Drosophila models of Freeman-Sheldon Syndrome. Biophysical Journal. In press.
- Guo, T., W.A. Kronert, K,H. Hsu, A. Huang, F. Sarsoza, K.M. Bell, J.A. Suggs, D.M. Swank and S.I. Bernstein (2020) Drosophila myosin mutants model the disparate severity of type 1 and type 2B distal arthrogryposis and indicate an enhanced actin affinity mechanism. Skeletal Muscle 10:24
- Viswanathan, M.C., W. Schmidt, P. Franz, M.J. Rynkiewicz, C.S. Newhard, A. Madan, W. Lehman, D.M. Swank, M. Preller and A. Cammarato (2020) A role for actin flexibility in thin filament-mediated contractile regulation and myopathy. Nature Commun. 11:2417.
- Guo, T., W.A. Kronert, K,H. Hsu, A. Huang, F. Sarsoza, K.M. Bell, J.A. Suggs, D.M. Swank and S.I. Bernstein (2020) Drosophila myosin mutants model the disparate severity of type 1 and type 2B distal arthrogryposis and indicate an enhanced actin affinity mechanism. Skeletal Muscle 10:24.
- Palmer, B.M., D.M. Swank, M.S. Miller, B.C.W. Tanner, M. Meyer, and M.M. LeWinter (2020) Enhancing diastolic function by strain-dependent detachment of cardiac myosin crossbridges. J. Gen. Physiol. 152:e201912484.
- Straight, C.R., K.M. Bell, J.N. Slosberg, M.S. Miller and D.M. Swank (2019) A myosin-based mechanism for stretch activation and its possible role revealed by varying phosphate concentration in fast and slow mouse skeletal muscle fibers. Am. J. Physiol. Cell Physiol. 317:C1143-1152.
- Bell, K.M., W.A. Kronert, A. Huang, S.I. Bernstein, and D.M. Swank (2019) The R249Q hypertrophic cardiomyopathy myosin mutation decreases contractility in Drosophila by impeding force production. J. of Physiology. 597:2403-2420.