Faculty & Staff
Alla Kostyukova, PhD
Alla Kostyukova, Ph.D.
Regulation of actin dynamics by actin-binding proteins; protein structure and protein-protein interactions; protein engineering; circular dichroism
Office: 340D Wegner Hall 📞509-335-1888
The Gene and Linda Voiland
School of Chemical Engineering and Bioengineering
1505 Stadium Way, Room 105
P.O. Box 646515
Washington State University
Pullman, WA 99164-6515
Dr. Dmitri Tolkatchev, Assistant Research Professor (2014-present)
Postdoctoral Research Associates
Dr. Natalia Moroz (2011-2015)
Current Graduate Students
Karla Bonic (REU)
Former Graduate Students
Mert Colpan (University of Arizona)
Kevin Gray (University of Maryland)
Kyle Swain (CP Kelco)
Tanzila Islam (Intel)
Thu (Lily) Ly (AGC Biologics)
Alla Kostyukova received her M.Sc. in Biophysics from St. Petersburg State University, Russia, and Ph.D. in Molecular Biology from the Institute of Protein Research, Russian Academy of Sciences & Moscow State University. She worked as a Research Associate in the Institute of Protein Research, Russia, and as a Senior Research Associate in RIKEN Harima Institute at SPring8, Japan, before moving to the USA. Before joining the Washington State University Voiland School faculty she worked for 4 years as an Assistant Professor and Director of the Circular Dichroism Facility in Robert Wood Johnson Medical School, Piscataway, NJ.
- Regulation of actin dynamics in cytoskeleton of muscle and non-muscle cells. Playing a critical role in muscle contraction, cell movement, and cell morphology, actin filaments form vastly different structures in different cell types and different locations within the cell. Regulation of the dynamics at actin’s ends is of central importance in the assembly of these various structures. The major goal of our research is to determine the mechanisms of this fine-tuned regulation necessary to understand processes existent in living cells, such as myocytes and neurons.
- Protein structure, protein-protein interactions and protein engineering. Important part of our research is studying structure of proteins and formation of protein complexes as well as engineering proteins with desired properties. These studies are parts in our ongoing projects as well as incollaborative projects.
Ongoing Research Projects
- NIH RO1 GM120137, 06/01/2017-05/31/2021
Regulation of the actin filament pointed end dynamics in health and disease.
List of Recent Publications
(full list of publications: https://goo.gl/m5ixoB )
(italic: graduate students, underlined: undergraduate students)
- Moraczewska J, Robaszkiewicz K, Śliwinska M, Czajkowska M, Ly T, Kostyukova, A.S., Wen H, Zheng W. Congenital myopathy-related mutations in tropomyosin disrupt regulatory function through altered actin affinity and tropomodulin binding. FEBS J. 2019 286(10):1877-1893.
- Ly T, Pappas CT, Johnson D, Schlecht W, Colpan, M, Galkin VE, Gregorio CC, Dong WJ, Kostyukova, A.S. Effects of cardiomyopathy-linked mutations k15n and r21h in tropomyosin on thin filament regulation and pointed-end dynamics. Mol Biol Cell. 2019;30(2):268-281.
- Hu H, Islam T, Kostyukova, A.S., Ha S, Gupta S. From Battery Enabled to Natural Harvesting: Enzymatic BioFuel Cell Assisted Integrated Analog Front-End in 130nm CMOS for Long-Term Monitoring. IEEE Transactions on Circuits and Systems – I: Regular Papers. 2018; 66(2):534-545.
- Gray, K.T.<, Stefen H, Ly TNA, Keller CJ, Colpan, M, Wayman GA, Pate E, Fath T, Kostyukova, A.S. Tropomodulin’s Actin-Binding Abilities Are Required to Modulate Dendrite Development. Front Mol Neurosci. 2018;11:357.
- Tolkatchev D, Elnatan D, Nogara L, Ly T, Naber N, Haak K, Meech R, Cooke R, Kostyukova, A.S. Piperine, an alkaloid inhibiting the super-relaxed state of myosin, binds to the myosin regulatory light chain. Arch Biochem Biophys. 2018; 659:75-84.
- Arslan B, Colpan, M, Gray, K.T., Abu-Lail NI, Kostyukova, A.S. Characterizing interaction forces between actin and proteins of the tropomodulin family reveals the presence of the N-terminal actin-binding site in leiomodin. Arch Biochem Biophys. 2018, 638:18-26.
- Ly T, Krieger I, Tolkatchev D, Krone C, Moural T, Samatey FA, Kang C, Kostyukova, A.S. Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H. Protein Sci. 2018, 27(2):498-508.
- Barker, C.S., Meshcheryakova, I.V., Kostyukova, A.S., Freddolino, P.L., Samatey, F.A. An intrinsically disordered linker controlling the formation and the stability of the bacterial flagellar hook. BMC Biol. 2017, 15(1):97.
- Colpan, M., Ly T., Grover, S., Tolkatchev, D., Kostyukova, A.S. The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics. Arch Biochem Biophys. 2017, 630:18-26.
- Ly T., Moroz, N.A., Pappas, C.T., Novak, S.M., Tolkatchev, D., Wooldridge, D., Mayfield, R.M., Helms, G., Gregorio, C.C., Kostyukova, A.S. The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2’s function. Molecular Biology of the Cell, 2016 27:16 2565-2575.
- Graça, T., Silva, M., Kostyukova, A.S., Palmer, G. Structural basis for recombinatorial permissiveness in the generation of Anaplasma marginale Msp2 antigenic variants. Infection and Immunity, 2016, 84(10):2740-7.
- Gray, K.T., Suchowerska, A.K., Bland, T., Colpan, M., Wayman, G., Fath, T., Kostyukova, A.S. Tropomodulin isoforms utilize specific binding functions to modulate dendrite development. Cytoskeleton, 2016; 73(6):316-28.
- Colpan, M., Moroz, N.A., Gray, K.T., Cooper, D.A., Diaz, C.A., Kostyukova, A.S. Tropomyosin-binding properties modulate competition between tropomodulin isoforms. Arch Biochem Biophys. 2016; 600:23-32.
- Arslan, B., Colpan, M., Ju, X., Zhang, X., Kostyukova, A.S., Abu-Lail, N. The effects of noncellulosic compounds on the nanoscale interaction forces measured between carbohydrate-binding module and lignocellulosic biomass. Biomacromolecules. 2016; 17(5):1705-15.
- Colpan, M., Tolkatchev, D., Grover, S., Helms, G.L., Cort, J., Moroz, N.A., Kostyukova, A.S. Localization of the Binding Interface between Leiomodin-2 and -Tropomyosin. Biochim Biophys Acta. 2016 1864(5):523-30.