Work and motion generation in muscle and non-muscle cells requires the transduction of chemical into mechanical energy. This function is carried out by a cellular cytoskeletal apparatus which contains actin and myosin, as well as many other proteins. The interactions between these proteins and the changes in their structure constitute the molecular basis for force generation and motile processes in systems as diverse as cardiac muscle and neuronal axons. Our goal of elucidating the mechanism of motile processes is pursued at two levels. At the molecular level we are concerned with the structural and dynamic properties of cytoskeletal proteins. We explore structure-function relationships in actin and actin binding proteins by biochemical, biophysical, immunochemical, and biological approaches. Various steps in the interactions of these proteins 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, the proteins which nucleate or terminate them, 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.
Grintsevich Elena E, Reisler Emil Drebrin Inhibits Cofilin-Induced Severing of F-Actin. Cytoskeleton (Hoboken). 2014 Aug 71:472-483.
Sharma Shivani, Grintsevich Elena E, Woo JungReem, Gurel Pinar S, Higgs Henry N, Reisler Emil, Gimzewski James K Nanostructured self-assembly of inverted formin 2 (INF2) and F-actin-INF2 complexes revealed by atomic force microscopy. Langmuir. 2014 Jul 1;30(25):7533-9.
Gurel Pinar S, Ge Peng, Grintsevich Elena E, Shu Rui, Blanchoin Laurent, Z. Hong Zhou, Reisler Emil, Higgs Henry N. INF2-mediated severing through actin filament encirclement and disruption. Curr Biol. 2014 Jan 20;24(2):156-64.
Chen Christine K, Benchaar Sabrina A, Phan Mai, Grintsevich Elena E, Loo Rachel R, Loo Joseph A, Reisler Emil Cofilin-induced changes in F-actin detected via cross-linking with benzophenone-4-maleimide. Biochemistry. 2013 Aug 13;52(32):5503-9.
Sharma Shivani, Zhu Huanqi Grintsevich Elena E, Reisler Emil, Gimzewski James K. Correlative nanoscale imaging of actin filaments and their complexes. Nanoscale. 2013 Jul 7;5(13):5692-702.
Mikati Mouna A, Grintsevich Elena E, Reisler Emil Drebrin-induced stabilization of actin filaments J Biol Chem. 2013 Jul 5;288(27):19926-38
Dmitri S. Kudryashov, Reisler Emil ATP and ADP actin states Biopolymers. 2013 Apr;99(4):245-56.
Hyeran Kang, Michael J. Bradley, Brannon R. McCullough, Anaëlle Pierre, Elena E. Grintsevich, Emil Reisler, Enrique M. De La Cruza Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness Proc Natl Acad Sci U S A. 2012 Oct 16;109(42),
Durer Zenep A, Kudryashov Dmitri S, Sawaya Michael R, Altenbach Christian, Hubbell Wayne, Reisler Emil Structural states and dynamics of the D-loop in actin. Biophys J. 2012 Sep 5;103(5):930-9.
Sharma Shivani, Grintsevich Elena E, Hsueh Carlin, Reisler Emil, Gimzewski James K Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin. Biophys J. 2012 Jul 18;103(2):275-83.
Chen Christine K, Sawaya Michael R, Phillips Martin L, Reisler Emil, Quinlan Margot E Multiple forms of Spire-actin complexes and their functional consequences. The Journal of Biological Chemistry, 2012; 287(13): 10684-92.
Sharma Shivani, Grintsevich Elena E, Phillips Martin L, Reisler Emil, Gimzewski James K Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution. Nano Letters, 2011; 11(2): 825-7.
Muhlrad Andras, Grintsevich Elena E, Reisler Emil Polycation induced actin bundles. Biophysical Chemistry, 2011.
Galkin Vitold E, Orlova Albina, Kudryashov Dmitri S, Solodukhin Alexander, Reisler Emil, Schröder Gunnar F, Egelman Edward H Remodeling of actin filaments by ADF/cofilin proteins. Proceedings of the National Academy of Sciences of the United States of America, 2011; 108(51): 20568-72.
Oztug Durer Zeynep A, Kamal J K Amisha, Benchaar Sabrina, Chance Mark R, Reisler Emil Myosin binding surface on actin probed by hydroxyl radical footprinting and site-directed labels. Journal of Molecular Biology, 2011; 414(2): 204-16.
McCullough Brannon R, Grintsevich Elena E, Chen Christine K, Kang Hyeran, Hutchison Alan L, Henn Arnon, Cao Wenxiang, Suarez Cristian, Martiel Jean-Louis, Blanchoin Laurent, Reisler Emil, De La Cruz Enrique M Cofilin-linked changes in actin filament flexibility promote severing. Biophysical Journal, 2011; 101(1): 151-9.
Kudryashov Dmitri S, Grintsevich Elena E, Rubenstein Peter A, Reisler Emil A nucleotide state-sensing region on actin. The Journal of Biological Chemistry, 2010; 285(33): 25591-601.
Grintsevich Elena E, Phillips Martin, Pavlov Dmitry, Phan Mai, Reisler Emil, Muhlrad Andras Antiparallel dimer and actin assembly. Biochemistry, 2010; 49(18): 3919-27.
Grintsevich Elena E, Galkin Vitold E, Orlova Albina, Ytterberg A Jimmy, Mikati Mouna M, Kudryashov Dmitri S, Loo Joseph A, Egelman Edward H, Reisler Emil Mapping of drebrin binding site on F-actin. Journal of Molecular Biology, 2010; 398(4): 542-54.
Oztug Durer Zeynep A, Diraviyam Karthikeyan, Sept David, Kudryashov Dmitri S, Reisler Emil F-actin structure destabilization and DNase I binding loop: fluctuations mutational cross-linking and electron microscopy analysis of loop states and effects on F-actin. Journal of Molecular Biology, 2010; 395(3): 544-57.
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. Cell Motililty 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
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