Dr. Elena Grintsevich

Research in the Grintsevich Lab focuses on regulation of actin cytoskeleton. Actin is a protein that plays a central role in supporting cell shape, mechanical properties, motility, cell signaling, intracellular transport, and other functions. How is it possible for one protein to have so many distinct cellular functions? Short answer is - actin is a team player. Actin cytoskeleton is tightly regulated by >150 different accessory proteins which are expressed and localized in a tissue-specific or/and developmentally-regulated manner to support various cellular functions. Some of these regulatory proteins and their interactions are extensively studied but many of them are poorly understood and largely uncharacterized.

Our goal is to advance the understanding of how actin is regulated in neuronal cells. It is recognized that many devastating neurodegenerative diseases are linked to misregulation of neuronal cytoskeleton. Indeed, functionality of the neuronal sub-structures such as dendritic spines and axonal growth cones is dependent on a tightly-controlled remodeling of actin cytoskeleton. The focus of our research is on the regulators of actin cytoskeleton that are linked to brain pathologies and development. Understanding of these regulatory interactions will create a window of opportunity for intervention in neurodegenerative diseases and normal aging.

We have excellent research opportunities for graduate and undergraduate students. Depending on the specific project, research students will learn a range of the molecular biology techniques, protein expression and purification, various biochemical assays, and microscopy data analysis.

We're recruiting! Three (3) graduate and three (3) undergraduate research positions are open. Please email me for more details.

1. Ginosyan A. A., Grintsevich E.E., Reisler E. Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly. (2019) Mol. Biol. Cell., 30 (5), 646-657; PMID:30625038
2. Grintsevich E.E., Ge P., Sawaya M.R., Yesilyurt H.G, Terman J.R., Zhou Z.H., Reisler E. Catastrophic disassembly of actin filaments via Mical-mediated oxidation. (2017) Nat. Commun., 8 (1), 2183; PMID: 29259197
3. Grintsevich E.E., Yesilyurt H.G., Rich S.K., Hung R.J., Terman J.R., Reisler E. F-actin dismantling through a redox-driven synergy between Mical and cofilin. (2016) Nat. Cell Biol., 18(8), 876-885; PMID:27454820; PMCID:PMC4966907
4. Ambrosi C., Ren C., Spagnol G., Cavin G., Cone A., Grintsevich E.E., Sosinsky G.E., Sorgen P.L. (2016) Connexin43 forms supramolecular complexes through non-overlapping binding sites for drebrin, tubulin, and ZO-1. PLoS One, 11(6), e0157073; PMID:27280719; PMCID:PMC4900556
5. Grintsevich E.E., Reisler E. (2014) Drebrin inhibits cofilin-induced severing of F-actin. Cytoskeleton (Hoboken). 71(8), 472-483; PMID:25047716; PMCID:PMC4465285
6. Mikati M.A., Grintsevich E.E., Reisler E. (2013) Drebrin-induced stabilization of actin filaments. J. Biol. Chem., 288(27), 19926-19938; PMID:23696644; PMCID:PMC3707693
7. Sharma S., Grintsevich E.E., Hsueh C., Reisler E., Gimzewski J.K. (2012) Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin. Biophys. J., 103(2), 275-283; PMID:22853905; PMCID:PMC3400778
8. Sharma S., Grintsevich E.E., Phillips M.L., Reisler E, Gimzewski J.K. (2011) Atomic force microscopy reveals drebrin induced remodeling of F-actin with subnanameter resolution. Nano Lett., 11(2), 825-827; PMID: 21175132
9. Grintsevich E.E., Galkin V.E., Orlova A., Ytterberg A.J., Mikati M.M., Kudryashov D.S., Loo J.A., Egelman E.H., Reisler E. (2010) Mapping of Drebrin Binding Site on F-Actin. J. Mol. Biol., 398(4), P. 542-554; PMID: 20347847; PMCID: PMC2866048. (Cover)

1. Grintsevich E.E. (2017) Chapter 5, Remodeling of actin filaments by drebrin A and its implications. In Drebrin (T. Shirao and Y. Sekino, Eds); Adv. Exp. Med. Biol., 1006, 61-82, Springer Japan KK, Tokyo
2. Grintsevitch E.E., Reisler, E. (2013) Chapter 4, Cytoskeleton Dynamics and Binding Factors. In The Cytoskeleton (R. Dermietzel, Ed.); Neuromethods 79, 63-83, New York: Humana Press