Alla Kostyukova, PhD

Biographical Information

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.

Research Interests

1. 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.
2. 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.
• NIH RO1 AR062279, 02/25/2016-04/30/2018
  Mechanisms Controlling the Super-Relaxed State.
• Office of Research, WSU, Grand Challenges Seed Grant, 06/01/2016-12/30/2017
  Next Generation Continuously Monitored Reusable Low-Cost Biochemical / Physiologic Sensors with Predictive Wireless Electronics Powered by Enzymatic Biofuel Cells.

List of Recent Publications

(full list of publications: https://goo.gl/m5ixoB )

1. Gray, K.T., Kostyukova, A.S., Fath, T. Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function. Mol Cell Neurosci. 2017. pii: S1044-7431(16)30207-X. doi: 10.1016/j.mcn.2017.04.002.
2. 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.
3. 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.
4. 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.
5. Colpan, M., Moroz, N.A., Gray, K.T., Cooper, D.A., Diaz, C.A., Kostyukova, A.S. Tropomyosin- and actin-binding properties of tropomodulins modulate their competition for binding at the pointed end of actin filaments. Arch Biochem Biophys. 2016; 600:23-32.
6. 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.
7. 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 α-Tropomyosin. Biochim Biophys Acta. 2016 1864(5):523-30.
8. van Dijk, S.J., Kooiker, K.B., Mazzalupo, S., Yang Y., Kostyukova, A.S., Mustacich, D.J., Hoye, E.R., Stern, J.A., Kittleson, M.D., Harris, S.P. The A31P missense mutation in cardiac myosin binding protein C alters protein structure but does not cause haploinsufficiency. Arch Biochem Biophys. 2016; 601:133-140.
9. Yuen M, Sandaradura SA, Dowling JJ, Kostyukova AS, Moroz N, Quinlan KG, Lehtokari VL, Ravenscroft G, Todd EJ, Ceyhan-Birsoy O, Gokhin DS, Maluenda J, Lek M, Nolent F, Pappas CT, Novak SM, D’Amico A, Malfatti E, Thomas BP, Gabriel SB, Gupta N, Daly MJ, Ilkovski B, Houweling PJ, Davidson AE, Swanson LC, Brownstein CA, Gupta VA, Medne L, Shannon P, Martin N, Bick DP, Flisberg A, Holmberg E, Van den Bergh P, Lapunzina P, Waddell LB, Sloboda DD, Bertini E, Chitayat D, Telfer WR, Laquerrière A, Gregorio CC, Ottenheijm CA, Bönnemann CG, Pelin K, Beggs AH, Hayashi YK, Romero NB, Laing NG, Nishino I, Wallgren-Pettersson C, Melki J, Fowler VM, MacArthur DG, North KN, Clarke NF. Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy. J Clin Invest. 2014; 124(11):4693-708.
10. Bliss KT, Tsukada T, Novak SM, Dorovkov MV, Shah SP, Nworu C, Kostyukova AS, Gregorio CC. Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle. FASEB J. 2014, 28:3987-3995.
11. Guillaud, L., Gray, K.T., Moroz, N., Pantazis, C., Pate, E., Kostyukova, A.S. The role of tropomodulin’s Leucine Rich Repeat domain in formation of neurite-like processes. Biochemistry 2014, 53(16):2689-700.
12. Galeva, A., Moroz, N., Yoon, YH., Hughes, K.T., Samatey, F.A., Kostyukova, A.S. Bacterial flagellin-specific chaperone FliS interacts with anti-sigma factor FlgM. J. Bacteriol. 2014, 196(6):1215.
13. Meshcheryakov, V.A., Barker, C.S., Kostyukova, A.S., Samatey, F.A. Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system. PLoS One. 2013;8(7):e68384.
14. Moroz, N., Novak, S.M., Azevedo, R., Colpan, M., Uversky, V.N., Gregorio, C.C., Kostyukova, A.S. Alteration of tropomyosin-binding properties of tropomodulin1 affects its capping ability and localization in skeletal myocytes. J. Biol. Chem. 2013, 288(7):4899–907.