Michael Ostap, PhD

Professor of Physiology

Director of the Pennsylvania Muscle Institute

Lab Web Site

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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

ostap@mail.med.upenn.edu

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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

  • 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.)


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