Abstract:
:Myosin VI is a molecular motor that is thought to function both as a transporter and as a cytoskeletal anchor in vivo. Here we use optical tweezers to examine force generation by single molecules of myosin VI under physiological nucleotide concentrations. We find that myosin VI is an efficient transporter at loads of up to ∼2 pN but acts as a cytoskeletal anchor at higher loads. Our data and the resulting model are consistent with an indirect coupling of global structural motions to nucleotide binding and release. The model provides a mechanism by which load may regulate the dual functions of myosin VI in vivo. Our results suggest that myosin VI kinetics are tuned such that the motor maintains a consistent level of mechanical tension within the cell, a property potentially shared by other mechanosensitive proteins.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Chuan P,Spudich JA,Dunn ARdoi
10.1016/j.jmb.2010.10.010subject
Has Abstractpub_date
2011-01-07 00:00:00pages
105-12issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(10)01107-1journal_volume
405pub_type
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