Perelman School of Medicine at the University of Pennsylvania

ROBERTO DOMINGUEZ, Ph.D.
Professor of Physiology

728 Clinical Research Building
415 Curie Boulevard
Philadelphia, PA 19104-6085
droberto@mail.med.upenn.edu

Phone: 215-573-4559
Lab: 215-573-0983
Fax: 215 573-2273
Lab web page:
http://www.med.upenn.edu/dominguez

Other Perelman School of Medicine Affiliations
Biochemistry and Molecular Biophysics Graduate Group

Pennsylvania Muscle Institute

Degrees
Ph.D., Pasteur Institute and Paris-Sud University, France, 1996,
M.S., Odessa State University, formerly-USSR, 1987

Honors
NIH Study Section (MSFC), 2006-present
Co-Chair Motility Subgroup of the Biophysical Society, 2006
American Heart Association, Established Investigator Award, 2002
American Heart Association, Grant-in-Aid Junior Investigator Award, 1999
March of Dimes, Basil O’Connor Scholar, 1998
Fellow of the German Academic Exchange Service (DAAD), 1992
Fellow of the Société Française de Belgique, 1989
Member of the Editorial Board of Biophysical Journal

Professional Affiliations
The American Society for Cell Biology
American Crystallographic Association
Biophysical Society
American Heart Association
American Association for the Advancement of Science

Research Description
The actin cytoskeleton plays an essential role in multiple cellular functions, including cytokinesis, vesicular trafficking and the maintenance of cell shape and polarity. To accomplish these functions, the cytoskeleton undergoes constant remodeling into various forms of structural and functional networks, such as lamellipodia, filopodia, stress fibers and focal adhesions. Remodeling of the cytoskeleton is a tightly regulated process, involving hundreds of actin-binding and signaling proteins. The main focus of the research in our lab is to understand the molecular basis for how protein-protein interaction networks bring together cytoskeleton scaffolding, nucleation, elongation, and signaling proteins to accomplish specific cellular functions.

Our primary research tool is protein X-ray crystallography. The atomic “snapshots” resulting from the X-ray crystal structures of proteins provide a wealth of knowledge, but lack information about the dynamic aspects of protein-protein interactions. To obtain this kind of information we also use a host of other approaches, including mutagenesis, bio-informatics, biophysical and biochemical methods.

Publications

Kast DJ, Yang C, Disanza A, Boczkowska M, Madasu Y, Scita G, Svitkina T and Dominguez R (2014) Molecular mechanism of IRSp53 regulation by autoinhibition and activation by Cdc42. Nature Struct Mol Biol. doi: 10.1038/nsmb.2781. [Epub ahead of print]

Boczkowska M, Rebowski G, Kast DJ, Dominguez R (2014) Structural analysis of the transitional state of Arp2/3 complex activation by two actin-bound WCAs. Nature Commun 5:3308. DOI:10.1038/ncomms4308

Turegun B, Kast D, Dominguez R (2013) Subunit Rtt102 controls the conformation of the Arp7/9 heterodimer and its interactions with nucleotide and the catalytic subunit of SWI/SNF remodelers. J Biol Chem DOI:10.1074/jbc.M113.514083

Zwolak A, Yang C, Feeser EA, Ostap EM, Svitkina T, Dominguez R (2013) CARMIL leading edge localization depends on a non-canonical PH domain and dimerization. Nature Commun 4:2523. DOI:10.1038/ncomms3523

Boczkowska M, Rebowski G, Dominguez R (2013) GMF interacts with Arp2/3 complex in a nucleotide state-dependent manner. J Biol Chem 288:25683-25688

Click here for a full list of publications
(searches the National Library of Medicine's PubMed database.)