Dr. Ali graduated (M.Sc.) in Physics from Aligarh Muslim University, India in 1993. He received his Ph.D degree in Biophysics from Toyohashi University of Technology, Japan in 2000. He worked as a Post Doctoral Fellow in the Department of Physics, Keio University and the Center for Integrative Bioscience, Okazaki National Research Institutes, Japan from 2000-2002. Then he returned to Bangladesh and worked as a faculty in the department of Physics, Shah Jalal University of Science and Technology, from 2002-2005. Dr. Ali worked as a post-doctoral researcher in the department of Molecular Physiology and Biophysics, University of Vermont from 2005-2008. Dr. Ali joined the UVM Faculty in 2008, and promoted to Assistant Professor in 2013.
Myosin, a motor protein, captures the energy from ATP hydrolysis to generate force and motion through its interactions with actin filaments in both muscle and non-muscle cells. However, it remains unclear how myosin converts chemical energy into mechanical movement. To address this question, I am studying a two-headed, processive myosin V molecular motor that moves along an actin filament over long distances. To understand the mechanism of force generation at a single molecule level, I am using quantum dots which are bound to each of the two heads of myosin V through a biotin-streptavidin linkage. I observe the movement of myosin V at different conditions using a TIRF microscope that provides both high spatial and time resolution. I am mainly interested in characterizing myosin Vs walking mechanism and conformational changes during its movement along an actin filament. Myosin V is implicated in organelle transport in neurons and must move within a dense intracellular cytoskeletal network that is composed of overlapping and crisscrossing actin, intermediate, and microtubular filaments. The microtubule network is believed to be used for long-range cargo transport through kinesins and dyneins while the actin filaments are used for short range transport through myosin motors. But the mechanism by which this transport is coordinated is still unclear and is the present focus of my research.
Faculty Highlighted Publications
Sladewski T, *Billington N, *Ali MY, Bookwalter C, Lu H, Krementsova EB. Schroer T. and Trybus KM. Recruitment of two dyneins to an mRNA-dependent Bicaudal D transport complex. ELife 7:1-29 (2018). (*Co-first author).
Krementsova EB., Furuta K., Oiwa K, Trybus KM and Ali, MY. Small teams of myosin Vc coordinate their stepping for efficient cargo transport on actin bundles J. Biol. Chem. 292(26): 10998 - 11008 (2017).
Lombardo A, Nelson SR, Ali, MY, Walcott S. Trybus KM, Warshaw DM. Myosin Va Motor Teams Maintain Their Heading When Transporting Vesicular Cargos in a Three-Dimensional Biomimetic Actin Cytoskeleton. Nature Communications. 8: 15692. (2017)
Ali MY, Vilfan A, Trybus KM, Warshaw DM. Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles. Biophys J. 111(10):2228-2240 (2016).
Mukherjea M, Ali MY, Kikuti C, Safer D, Yang Z, Sirkia H, Ropars V, Houdusse A, Warshaw DM, Sweeney HL. Myosin VI must dimerize and deploy its unusual lever arm in order to perform its cellular roles. Cell Rep.; 8(5): 1522-32. (2014)
Ali MY, Previs S, Nelson SR, Trybus KM, Sweeney HL, Warshaw DM. Stepping dynamics of myosin V and myosin VI when transport cargo along actin-actin intersections and bundles. Traffic 14, 70-81 (2013).
Ali MY, Kennedy GG, Safer S, Trybus KM, Sweeney HL, Warshaw DM. Myosin Va and myosin VI coordinate their steps while engaged in an in vitro tug of war during cargo transport. Proc. Natl. Acad. Sci. U. S. A. 108 (34), E535-41 (2011).
Ali MY, Lu H, Bookwalter CS, Warshaw DM, Trybus KM. Myosin V and Kinesin act as tethers to enhance each others' processivity. Proc. Natl. Acad. Sci. U. S. A. 105(12), 4691-6 (2008).