How the load and the nucleotide state affect the actin filament binding mode of the molecular motor myosin V Export

@article{Mikhailenko:08aa, abstract = {The interaction between actin and myosin V has been probed by measuring the unbinding force of individual actomyosin complexes using optical tweezers. Surprisingly, we found that in both the nucleotide-free and ADP-bound states single- and double-headed binding occurs with approxi- mately the same probability. Estimation of the spring constant of individual actomyosin complexes confirmed that in each of the nucleotide states two distinct populations exist. These results confirm that optical nanometry can be used to reliably study the mechanism of how cytoskeleton molecular motors interact with their associated polymer lattices under solution conditions more closely resembling the intracellular environment.}, author = {Mikhailenko, S. V. and Oguchi, Y. and Ohki, T. and Shimozawa, T. and Olivares, A. O. and De La and Ishiwata, S.}, citeulike-article-id = {4571340}, journal = {J. Korean Phy. Soc.}, keywords = {actin, cell-division, myosin}, pages = {1726--1730}, posted-at = {2009-05-21 18:17:38}, priority = {2}, title = {How the load and the nucleotide state affect the actin filament binding mode of the molecular motor myosin V}, volume = {53}, year = {2008} }

TY - JOUR ID - Mikhailenko:08aa L3 - citeulike-article-id:4571340 N2 - The interaction between actin and myosin V has been probed by measuring the unbinding force of individual actomyosin complexes using optical tweezers. Surprisingly, we found that in both the nucleotide-free and ADP-bound states single- and double-headed binding occurs with approxi- mately the same probability. Estimation of the spring constant of individual actomyosin complexes confirmed that in each of the nucleotide states two distinct populations exist. These results confirm that optical nanometry can be used to reliably study the mechanism of how cytoskeleton molecular motors interact with their associated polymer lattices under solution conditions more closely resembling the intracellular environment. JF - J. Korean Phy. Soc. EP - 1730 TI - How the load and the nucleotide state affect the actin filament binding mode of the molecular motor myosin V VL - 53 SP - 1726 KW - actin KW - cell-division KW - myosin AU - Mikhailenko, SV AU - Oguchi, Y AU - Ohki, T AU - Shimozawa, T AU - Olivares, AO AU - De La AU - Ishiwata, S PY - 2008/// ER -