Mike Previs, Ph.D.

Assistant Professor  

Previs, Michael


Dr. Previs received his Ph.D. from the Cell and Molecular Biology Program at the University of Vermont in 2010, with research emphasis on the development of quantitative mass spectrometry-based proteomic techniques to examine muscle structure. Dr. Previs pursued his interest in muscle as a Post-doctoral Associate in the Molecular Physiology & Biophysics Department. In this role he developed single molecule assays to examine the molecular mechanics which underlie muscle function. In 2014, Dr. Previs was promoted to Assistant Professor of Molecular Physiology & Biophysics and is now establishing his own independent research program. Dr. Previs' lab uses a combination of mass spectrometry-based proteomic strategies and state-of-the-art single molecule imaging techniques to characterize the structure and function of muscle protein complexes in health and disease.


HSRF 108

HSRF 125

Lab Website

Lab Team

Neil Wood

Colleen Kelly


Research Description

My current research interests are focused on understanding the molecular mechanisms by which myosin binding protein C, a key muscle protein regulates the hearts ability to contract. The heart contracts on a beat-to-beat basis through orchestrated interactions of electrical, chemical and mechanical elements within the sarcomere, the elementary contractile unit. Ultimately, cardiac contraction results from sarcomere shortening due the sliding of actin-based thin filaments past myosin-based thick filaments. Myosin binding protein C is a thick-filament associated regulator of actomyosin sliding, and we have shown that is exerts its functional effects through direct interactions between both the actin- and myosin-based filamentous systems. My current studies are focused on further defining the binding partners involved in these regulatory interactions, and building complexity into my in vitro model systems to understand myosin binding protein C's function in the presence of additional actomyosin regulatory components which exist within the sarcomere. This work will continue to provide insight why mutations in myosin binding protein C's gene (MYBPC3) are a leading cause of heart disease including hypertrophic cardiomyopathy.

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