Myosin 19 : Biochemical Analysis of a Mitochondrial Associated Myosin
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Adikes et al., 2013
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Illustration by Sarah Friday from Adikes et al., 2013
I worked with Dr. Omar Quintero at Mount Holyoke College and Penn State Hershey. The Quintero lab is interested in understanding the role of the actin based motor proteins, myosins, in mitochondrial movement. The lab previously discovered that myosin 19 (MYO19) co-localizes with mitochondria and thus could potentially play an important role in mitochondrial movement. Using Fluorescence Recovery After Photobleaching (FRAP) I determined that MYO19 exchanges slowly with other cellular pools indicating that MYO19 is tightly associated with the mitochondrial outer membrane. To further understand the mechanism of actin-based mitochondrial positioning in cells I probed the biochemical properties of this motor. In vitro studies of MYO19 revealed a slow rate of ATP turn over and suggested a medium affinity for actin, indicating that MYO19 is either a slow motor or an actin-based mitochondrial anchor. To determine if there were regions of MYO19 that could lead to these biochemical properties I performed sequence
alignments, charge determination and structural predictions of the motor domain. I was able to identify specific amino acids in the MYO19 motor that I hypothesize correlate to the observed biochemical data.

Publications:
Adikes, R.C., Unrath W.C., Yengo, C.M., and Quintero, O.A. Biochemical analysis of the myosin-XIX motor domain. Cytoskeleton 70(5), 281-9.
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Quintero, O.A., DiVito, M.M., Adikes, R.C., Kortan, M.B., Case, L.B., Lier, A.J., Panaretos, N.S., Slater S.Q., Rengarajan, M., Feliu M., Cheney R.E. (2009) Human myo19 is a novel myosin that associates with mitochondria. Current Biology 19, 2008-2013.
Thin Filament Regulation
​I worked with Dr. Ned Debold at UMass Amherst. The goal of this project was to combine the expression of mutant proteins with the functional assays to probe the structure/function relationship of proteins that are crucial to proper muscle and heart function. My experiments focused on determining the effects of a cardiomyopathy causing mutations in TnT, a subunit of the muscle regulatory protein troponin, on the regulation of actomyosin motility. As the lead person on this project I had the opportunity to teach other members of the lab basic DNA cloning, molecular biology techniques and epiflourescence microscopy.
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Garland Publishing 1999