Michael Ostap, PhD
Professor of Physiology
Director of the Pennsylvania Muscle Institute
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700A Clinical Research Building
415 Curie Boulevard
Philadelphia, PA 19104
215-573-9758
Lab: 215-898-3685
Fax: 215-573-2273
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Michael Ostap, PhD
Professor of Physiology
Other Perelman School of Medicine Affiliations
Degrees & Education
BS, Chemistry, Illinois State University, 1988
PhD, Biochemistry, University of Minnesota, 1993
Awards & Honors
MERIT AWARD, National Institute of General Medical Sciences, NIH
Established Investigator, American Heart Association
American Heart Association, Scientist Development Grant
NIH Molecular Biophysics Training Grant
Damon Runyon-Walter Winchell Fellow
Mary L. Smith Award for Cardiovascular Research
Professional Affiliations
American Society for Cell Biology
Biophysical Society
Research Interests
Cell Motility, Muscle Contraction, Biochemical Kinetics, Cell Biophysics
Research Description
The long-range goal of my research is to understand the function, regulation, and molecular mechanism of myosin-I, a membrane-based molecular motor, in Cell Motility and transport. It is believed that myosin-I plays an integral role in the dynamic organization and transport of plasma and intracellular membranes. This type of membrane-based motility is essential in normal (e.g., amoebas and macrophages) and pathological cells (e.g., metastatic cancer cells) for several crucial cell functions including endocytosis, membrane trafficking, osmoregulation, and whole Cell Motility.
Despite intensive study, the physiological roles and molecular mechanisms of myosin-I have remained a mystery, in large part, because a single cell expresses several isoforms of myosin-I with (apparently) similar biochemical properties. To better define the individual roles of the myosin-I isoforms, we are using a rigorous interdisciplinary approach (combining chemistry, biophysics, cell, and molecular biology) to investigate the actual molecular machinery that is responsible for cell movements. We are obtaining a physical framework in which to discuss myosin-I function by investigating the enzymatic and structural properties of native and recombinant myosin-I isoforms, and we are investigating the in vivo localization, organization, dynamics, and physiology of myosin-I in fixed and live cells using high-resolution microscopy techniques. The correlation of the chemical and physical properties of myosin-I with the cellular dynamics will allow us to better define the physiological roles and molecular mechanisms of myosin-I.
Click here for a full list of publications.
(searches the National Library of Medicine's PubMed database.)
