article · 03/07/2012
The Highly Processive Kinesin-8, Kip3, Switches Microtubule Protofilaments with a Bias toward the Left
Résumé
Kinesin-1 motor proteins walk parallel to the protofilament axes of microtubules as they step from one tubulin dimer to the next. Is protofilament tracking an inherent property of processive kinesin motors, like kinesin-1, and what are the structural determinants underlying protofilament tracking? To address these questions, we investigated the tracking properties of the processive kinesin-8, Kip3. Using in vitro gliding motility assays, we found that Kip3 rotates microtubules counterclockwise around their longitudinal axes with periodicities of similar to 1 mu m. These rotations indicate that the motors switch protofilaments with a bias toward the left. Molecular modeling suggests 1), that the protofilament switching may be due to kinesin-8 having a longer neck linker than kinesin-1, and 2), that the leftward bias is due the asymmetric geometry of the motor neck linker complex.
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Bormuth, V., Nitzsche, B., Ruhnow, F., Mitra, A., Storch, M., Rammner, B., Howard, J., & Diez, S. (2012). The Highly Processive Kinesin-8, Kip3, Switches Microtubule Protofilaments with a Bias toward the Left. Biophys. J., 103(1). https://doi.org/10.1016/j.bpj.2012.05.024@article{Bormuth2012_129,
author = {Bormuth, Volker and Nitzsche, Bert and Ruhnow, Felix and Mitra, Aniruddha and Storch, Marko and Rammner, Burkhard and Howard, Jonathon and Diez, Stefan},
year = {2012},
month = {7},
title = {The Highly Processive Kinesin-8, Kip3, Switches Microtubule Protofilaments with a Bias toward the Left},
journal = {Biophys. J.},
publisher = {CELL PRESS},
volume = {103},
number = {1},
address = {600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA},
abstract = {Kinesin-1 motor proteins walk parallel to the protofilament axes of microtubules as they step from one tubulin dimer to the next. Is protofilament tracking an inherent property of processive kinesin motors, like kinesin-1, and what are the structural determinants underlying protofilament tracking? To address these questions, we investigated the tracking properties of the processive kinesin-8, Kip3. Using in vitro gliding motility assays, we found that Kip3 rotates microtubules counterclockwise around their longitudinal axes with periodicities of similar to 1 mu m. These rotations indicate that the motors switch protofilaments with a bias toward the left. Molecular modeling suggests 1), that the protofilament switching may be due to kinesin-8 having a longer neck linker than kinesin-1, and 2), that the leftward bias is due the asymmetric geometry of the motor neck linker complex.},
url = {http://www.dx.doi.org/10.1016/j.bpj.2012.05.024},
doi = {10.1016/j.bpj.2012.05.024},
issn = {0006-3495},
}TY - JOUR
AU - Bormuth, Volker
AU - Nitzsche, Bert
AU - Ruhnow, Felix
AU - Mitra, Aniruddha
AU - Storch, Marko
AU - Rammner, Burkhard
AU - Howard, Jonathon
AU - Diez, Stefan
PY - 2012
DA - 2012/07/03
TI - The Highly Processive Kinesin-8, Kip3, Switches Microtubule Protofilaments with a Bias toward the Left
JO - Biophys. J.
VL - 103
IS - 1
PB - CELL PRESS
SN - 0006-3495
AB - Kinesin-1 motor proteins walk parallel to the protofilament axes of microtubules as they step from one tubulin dimer to the next. Is protofilament tracking an inherent property of processive kinesin motors, like kinesin-1, and what are the structural determinants underlying protofilament tracking? To address these questions, we investigated the tracking properties of the processive kinesin-8, Kip3. Using in vitro gliding motility assays, we found that Kip3 rotates microtubules counterclockwise around their longitudinal axes with periodicities of similar to 1 mu m. These rotations indicate that the motors switch protofilaments with a bias toward the left. Molecular modeling suggests 1), that the protofilament switching may be due to kinesin-8 having a longer neck linker than kinesin-1, and 2), that the leftward bias is due the asymmetric geometry of the motor neck linker complex.
DO - 10.1016/j.bpj.2012.05.024
UR - http://www.dx.doi.org/10.1016/j.bpj.2012.05.024
ER -