Work done by muscle and non-muscle cells requires the transduction of
chemical into mechanical energy. This function is carried out by a cellular
contractile apparatus which contains actin and myosin as well as other
proteins. The interactions between these proteins and the changes in their
structure constitute the molecular basis for force generation in muscle and
non-muscle cells. Our goal of elucidating the mechanism of contractile
processes is pursued at two levels. At the molecular level we are concerned
with the structural and dynamic properties of the contractile proteins.
We explore structure-function relationships in actin, myosin and other
proteins by biochemical, biophysical, immunochemical, and biological approaches.
Intermediate steps in the contractile process are probed with the help of
nucleotide analogues, specific antibodies, synthetic peptides, and appropriate
mutants of the key proteins. At the cellular level, we study the function,
interactions, and structural transitions of assembled protein systems.
Many filamentous cellular structures are constructed from their components
through fine-tuned assembly processes. The biological function of these
filaments is frequently linked to the regulation of this assembly by cellular
factors. Our interest is focused on the formation of myosin and actin filaments
from their monomeric protein units. The mechanisms of the assembly reactions and
the structural changes which govern the polymerization reactions are studied by
biophysical, biochemical, and electron microscopy methods. To understand the
regulation of actin and myosin assembly by other proteins, macromolecular
contact sites are investigated by a wide spectrum of experimental techniques.
Scoville Damon, Stamm John D, Altenbach Christian, Shvetsov Alexander, Kokabi Kaveh, Rubenstein Peter A, Hubbell Wayne L, Reisler Emil. Effects of binding factors on structural elements in F-actin. Biochemistry, 2009; 48(2): 370-8.
Shvetsov Alexander, Berkane Emir, Chereau David, Dominguez Roberto, Reisler Emil. The actin-binding domain of cortactin is dynamic and unstructured and affects lateral and longitudinal contacts in F-actin. Cell motility and the cytoskeleton. 2009; 66(2): 90-8.
Shvetsov Alexander, Galkin Vitold E, Orlova Albina, Phillips Martin, Bergeron Sarah E, Rubenstein Peter A, Egelman Edward H, Reisler Emil. Actin hydrophobic loop 262-274 and filament nucleation and elongation. Journal of molecular biology, 2008; 375(3): 793-801.
Kudryashov Dmitri S, Cordero Christina L, Reisler Emil, Satchell Karla J Fullner. Characterization of the enzymatic activity of the actin cross-linking domain from the Vibrio cholerae MARTX Vc toxin. The Journal of biological chemistry, 2008; 283(1): 445-52.
Kudryashov Dmitri S, Durer Zeynep A Oztug, Ytterberg A Jimmy, Sawaya Michael R, Pashkov Inna, Prochazkova Katerina, Yeates Todd O, Loo Rachel R Ogorzalek, Loo Joseph A, Satchell Karla J Fullner, Reisler Emil. Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proceedings of the National Academy of Sciences of the United States of America, 2008; 105(47): 18537-42.
Grintsevich Elena E, Benchaar Sabrina A, Warshaviak Dora, Boontheung Pinmanee, Halgand Frédéric, Whitelegge Julian P, Faull Kym F, Loo Rachel R Ogorzalek, Sept David, Loo Joseph A, Reisler Emil. Mapping the cofilin binding site on yeast G-actin by chemical cross-linking. Journal of molecular biology, 2008; 377(2): 395-409.
Department of Chemistry & Biochemistry
UCLA
Box 951569 (post)
607 Charles E. Young Drive East (courier)
Los Angeles, CA 90095-1569
PI
Professor Emil Reisler reisler@mbi.ucla.edu
Postdoctoral Fellows
Zeynep Durer zeynep@chem.ucla.edu
Elena Grintsevich egrin@ucla.edu
Dimitri Koudriachov dkudryas@ucla.edu
Graduate Students
Christine Chen christinekchen@gmail.com
Michael Mcsunas mcsunasm@ucla.edu
Mouna Mikati mmikati@ucla.edu
Undergraduate Students
Johnny Cai johnnycai123@gmail.com
Sanjali Kumar keepdancing1000@ucla.edu
Yan Qin qindoris@ucla.edu
Lab Manager
Pamchal Faroghi pamchal@ucla.edu
