Roberto Dominguez, PhD
William Maul Measey Presidential Professor of Physiology II
Department: Physiology
Graduate Group Affiliations
Contact Information
Department of Physiology
Perelman School of Medicine
University of Pennsylvania
728 Clinical Research Bldg
415 Curie Blvd
Philadelphia, PA 19104-6085
Office: 215-573-4559
Fax: 215-573-2273
Email: droberto@pennmedicine.upenn.edu
I3H Keywords
- Innate and Adaptive Immunity to Pathogens
Publications
Links
Education
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M.S. (Theoretical Physics & Mathematics)
Faculty of Physics, Odessa State University (former USSR), 1987 -
Ph.D. (Protein Crystallography and Biochemistry)
Pasteur Institute and Paris-Sud University, Paris, France, 1996
Post-Graduate Training
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Pre-doctoral Trainee
University of Liége, Liége, Belgium, 1989 - 1991 -
Pre-doctoral Trainee
European Molecular Biology Laboratory, Heidelberg, Germany, 1992 - 1993 -
Graduate Student
Pasteur Institute, Paris, France, 1993 - 1996 -
Postdoctoral Fellow (structural biology)
Rosenstiel Center, Brandeis University, MA, 1996 - 1998
Description of Research Expertise
My laboratory studies the proteins that control the actin cytoskeleton and cytoskeleton-membrane connections, as well as the signaling cascades that regulate their activities. We use a broad spectrum of experimental approaches, spanning structural biology, biochemistry and cell biology, allowing us to correlate structure to function.
Cytoskeletal proteins control a myriad of fundamental cellular activities, including cell locomotion, intracellular transport, endo- and exocytosis. Dysfunction of cytoskeletal components is often associated with devastating diseases, such as cancer and several muscular, immune and neurodegenerative disorders.
Cytoskeletal proteins often form large functional assemblies, and additionally associate with cellular membranes. Therefore, our goal is to study their structures and activities within the context of such protein-protein and protein-membrane interaction networks. An important tool in our research is X-ray crystallography. The atomic “snapshots” resulting from crystal structures provide a wealth of knowledge, but lack information about the dynamic aspects of protein function. To obtain this kind of information we use a host of other approaches, including molecular biology, bioinformatics, biophysical methods (ITC, MALS, FRET, TIRF, Cryo-EM), and cell biology.