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Workshop / Seminar

CHE 598 Seminar: Leiomodin and the Control of Thin Filament Length in Muscle Cells

Spark
Spark 335 - Pullman Campus TFLO 247 - Tri-Cities Campus
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About the event

SPEAKER: Dr. Alla Kostyukova, Professor, WSU Voiland School of Chemical Engineering and Bioengineering

BIOGRAPHY:

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 several years as an Assistant Professor and Director of the Circular Dichroism Facility at Robert Wood Johnson Medical School, Piscataway, NJ. Dr. Kostyukova’s research interests include protein structure, protein-protein interactions, and protein engineering, with a focus on the regulation of actin dynamics in the cytoskeleton of muscle and non-muscle cells. The major goal of her research is to elucidate the mechanisms underlying this finely tuned regulation, which is essential for understanding processes in living cells, such as myocytes and neurons. Her work has been supported by several NIH grants, and she has published more than 75 peer-reviewed papers in this area.

 

ABSTRACT:

This talk will highlight recent advances in understanding the role of an actin-binding protein leiomodin in regulating thin filament length, which is essential for proper muscle contraction.  Structural, biochemical, and cellular studies collectively support a model in which leiomodin acts as a multifunctional regulator that promotes thin filament elongation while coordinating with other key proteins. Most recent studies show that leiomodin attaches to specific regions of the thin filament in a calcium-dependent manner and that even small changes in its interactions with other muscle proteins can affect its ability to regulate the thin filament length. Together, these findings highlight how delicate molecular interactions fine-tune the structure of muscle cells and are critical for healthy muscle function.