Other Perelman School of Medicine Affiliations
and Molecular Biophysics Graduate Group
Ph.D., Pasteur Institute and Paris-Sud University, France,
M.S., Odessa State University, formerly-USSR, 1987
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
The American Society for Cell Biology
American Crystallographic Association
American Heart Association
American Association for the Advancement of Science
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
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.
Boczkowska M, Rebowski G, Petoukhov MV, Hayes DB, Svergun DI, Dominguez R. Solution Structure of Activated Arp2/3 Complex by X-ray Scattering. Structure (2008) 16:695-704.
Chereau D, Boczkowska M, Skwarek-Maruszewska, A, Fujiwara I, Rebowski G, Hayes DB, Lappalainen P, Pollard TD, Dominguez R. Leiomodin is an actin filament nucleator in muscle cells. Science (2008) 320:239-243
F, Rebowski G, Lee SH & Dominguez R (2007).
Structural basis for the recruitment of profilin–actin
complexes during filament elongation by Ena/VASP. EMBO
SH, Hayes DB, Rebowski G, Tardieux I and Dominguez R
(2007). Toxofilin from Toxoplasma gondii forms a ternary
complex with an antiparallel actin dimer. PNAS 104:16122-16127.
R (2007). The b-Thymosin/WH2 Fold: Multifunctionality
and Structure. Ann
N Y Acad Sci. 1112:86-94.
SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R
(2007). Structural basis for the actin-binding function
of Missing-in-Metastasis. Structure 15:145-55.
E, Kerff F, Lee SH, Ferron F, Li Y, Dominguez R (2006).
Crystal structure of the actin-binding domain of alpha-actinin
1: evaluating two competing actin-binding models. J Struct Biol. 155:230-238.
D, Kerff F, Graceffa P, Grabarek Z, Langsetmo K, Dominguez
R (2005). Actin-bound structures of Wiskott-Aldrich syndrome
protein (WASP)-homology domain 2 and the implications
for filament assembly. PNAS 102:16644-16649.
Dominguez R (2004). Actin-binding proteins - a unifying
Biochem Sci. 29:572-578.
M, Kerff F, Langsetmo K, Tao T, Dominguez R (2004). Structural
basis of protein phosphatase 1 regulation. Nature 429:780-784.
Otterbein LR, Graceffa P, Dominguez R (2001). The crystal
structure of uncomplexed actin in the ADP state. Science 293:708-711.
Click here for
a full list of publications
(searches the National Library of Medicine's PubMed database.)