| Structural highlights
Function
[MYO5C_HUMAN] May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues.
Publication Abstract from PubMed
Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles.
The myosin X motor is optimized for movement on actin bundles.,Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, Liu X, Hissier P, Samazan F, Amigues B, Yang ED, Park H, Pylypenko O, Cecchini M, Sindelar CV, Sweeney HL, Houdusse A Nat Commun. 2016 Sep 1;7:12456. doi: 10.1038/ncomms12456. PMID:27580874[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, Liu X, Hissier P, Samazan F, Amigues B, Yang ED, Park H, Pylypenko O, Cecchini M, Sindelar CV, Sweeney HL, Houdusse A. The myosin X motor is optimized for movement on actin bundles. Nat Commun. 2016 Sep 1;7:12456. doi: 10.1038/ncomms12456. PMID:27580874 doi:http://dx.doi.org/10.1038/ncomms12456
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