| First Author | Fan Y | Year | 2012 |
| Journal | J Cell Biol | Volume | 198 |
| Issue | 1 | Pages | 47-55 |
| PubMed ID | 22778278 | Mgi Jnum | J:190753 |
| Mgi Id | MGI:5449655 | Doi | 10.1083/jcb.201111088 |
| Citation | Fan Y, et al. (2012) Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells. J Cell Biol 198(1):47-55 |
| abstractText | 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. |
