Poster abstracts
Poster number 122 submitted by Isabella Kolodny
Isoform-Specific Fine-Tuning of Nonmuscle Myosin-2A by the Essential Light Chain
Isabella M. Kolodny (Molecular, Cellular, and Developmental Biology Graduate Program), Charlotte Rose (Department of Physiology and Cell Biology, College of Medicine, The Ohio State University Wexner Medical Center, Columbus, OH, USA.), Angelina Ramirez-Navarro (Department of Physiology and Cell Biology, College of Medicine, The Ohio State University Wexner Medical Center, Columbus, OH, USA.), Giovanna Grandinetti, Krishna Chinthalapudi (Department of Physiology and Cell Biology, College of Medicine, The Ohio State University Wexner Medical Center, Columbus, OH, USA.), Sarah M. Heissler (Department of Physiology and Cell Biology, College of Medicine, The Ohio State University Wexner Medical Center, Columbus, OH, USA.)
Abstract:
Nonmuscle myosin-2A (NM2A) is a conventional myosin motor protein that generates
contractile force through ATP-dependent interactions with actin filaments to drive
essential cellular processes including cytokinesis, cell adhesion, and
migration. The NM2A holoenzyme comprises two heavy chains, two regulatory light
chains (RLCs), and two essential light chains (ELCs). Myosin light chains are
small EF-hand proteins that are important for both the structural integrity and
regulation of the holoenzyme. While the human genome encodes multiple ELC
isoforms, their specific contributions to the enzymatic properties of NM2A remain
largely unexplored. Here, we examined how two ELC isoforms, MYL6 and MYL6B,
influence NM2A motor function using biochemical and structural approaches. We found that the presence of different ELCs alters protein stability and fine-tunes kinetic signatures while preserving the overall structure of the holoenzyme. These
results suggest that varying light chain composition provides cells with a
mechanism to fine-tune NM2A motor function to specific physiological demands.
Keywords: Myosin, Cytoskeleton, Cryo-EM