Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells
Year: 2012
Type: article
Abstract: Addition of actin monomer (G-actin) to growing actin filaments (F-actin) at the leading edge generates force for cell locomotion. The polymerization reaction and its regulation have been studied in depth. However, the mechanism responsible for transport of G-actin substrate to the cell front is largely unknown; random diffusion, facilitated transport via myosin II contraction, local synthesis as a result of messenger ribonucleic acid localization, or F-actin turnover all might contribute. By tracking a photoactivatable, nonpolymerizable actin mutant, we show vectorial transport of G-actin in live migrating endothelial cells (ECs). Mass spectrometric analysis identified Myo1c, an unconventional F-actin-binding motor protein, as a major G-actin-interacting protein. The cargo-binding tail domain of Myo1c interacted with G-actin, and the motor domain was required for the transport. Local microinjection of Myo1c promoted G-actin accumulation and plasma membrane ruffling, and Myo1c knockdown confirmed its contribution to G-actin delivery to the leading edge and for cell motility. In addition, there is no obvious requirement for myosin II contractile-based transport of G-actin in ECs. Thus, Myo1c-facilitated G-actin transport might be a critical node for control of cell polarity and motility.
Source: The Journal of Cell Biology
Institutions: Cleveland Clinic, Cleveland Clinic Research
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: hybrid
Awards: Global analysis of mRNA polarization in migrating endothelial cells, Oxidation in Inflammation and Cardiovascular Disease, Mechanisms linking inflammation, metabolism, and atherosclerosis., Membrane Polarization and Endothelial Cell Motility, Clinical and Translational Science Collaborative of Cleveland
OpenAlex ID: W2111234184