article · 04/06/2013
Kinesin-8 Is a Low-Force Motor Protein with a Weakly Bound Slip State
Résumé
During the cell cycle, kinesin-8s control the length of microtubules by interacting with their plus ends. To reach these ends, the motors have to be able to take many steps without dissociating. However, the underlying mechanism for this high processivity and how stepping is affected by force are unclear. Here, we tracked the motion of yeast (Kip3) and human (Kif18A) kinesin-8s with high precision under varying loads using optical tweezers. Surprisingly, both kinesin-8 motors were much weaker compared with other kinesins. Furthermore, we discovered a force-induced stick-slip motion: the motor frequently slipped, recovered from this state, and then resumed normal stepping motility without detaching from the nnicrotubule. The low forces are consistent with kinesin-8s being regulators of microtubule dynamics rather than cargo transporters. The weakly bound slip state, reminiscent of a molecular safety leash, may be an adaptation for high processivity.
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Jannasch, A., Bormuth, V., Storch, M., Howard, J., & Schaeffer, E. (2013). Kinesin-8 Is a Low-Force Motor Protein with a Weakly Bound Slip State. Biophys. J., 104(11). https://doi.org/10.1016/j.bpj.2013.02.040@article{Jannasch2013_128,
author = {Jannasch, Anita and Bormuth, Volker and Storch, Marko and Howard, Jonathon and Schaeffer, Erik},
year = {2013},
month = {6},
title = {Kinesin-8 Is a Low-Force Motor Protein with a Weakly Bound Slip State},
journal = {Biophys. J.},
publisher = {CELL PRESS},
volume = {104},
number = {11},
address = {600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA},
abstract = {During the cell cycle, kinesin-8s control the length of microtubules by interacting with their plus ends. To reach these ends, the motors have to be able to take many steps without dissociating. However, the underlying mechanism for this high processivity and how stepping is affected by force are unclear. Here, we tracked the motion of yeast (Kip3) and human (Kif18A) kinesin-8s with high precision under varying loads using optical tweezers. Surprisingly, both kinesin-8 motors were much weaker compared with other kinesins. Furthermore, we discovered a force-induced stick-slip motion: the motor frequently slipped, recovered from this state, and then resumed normal stepping motility without detaching from the nnicrotubule. The low forces are consistent with kinesin-8s being regulators of microtubule dynamics rather than cargo transporters. The weakly bound slip state, reminiscent of a molecular safety leash, may be an adaptation for high processivity.},
url = {http://www.dx.doi.org/10.1016/j.bpj.2013.02.040},
doi = {10.1016/j.bpj.2013.02.040},
issn = {0006-3495},
}TY - JOUR
AU - Jannasch, Anita
AU - Bormuth, Volker
AU - Storch, Marko
AU - Howard, Jonathon
AU - Schaeffer, Erik
PY - 2013
DA - 2013/06/04
TI - Kinesin-8 Is a Low-Force Motor Protein with a Weakly Bound Slip State
JO - Biophys. J.
VL - 104
IS - 11
PB - CELL PRESS
SN - 0006-3495
AB - During the cell cycle, kinesin-8s control the length of microtubules by interacting with their plus ends. To reach these ends, the motors have to be able to take many steps without dissociating. However, the underlying mechanism for this high processivity and how stepping is affected by force are unclear. Here, we tracked the motion of yeast (Kip3) and human (Kif18A) kinesin-8s with high precision under varying loads using optical tweezers. Surprisingly, both kinesin-8 motors were much weaker compared with other kinesins. Furthermore, we discovered a force-induced stick-slip motion: the motor frequently slipped, recovered from this state, and then resumed normal stepping motility without detaching from the nnicrotubule. The low forces are consistent with kinesin-8s being regulators of microtubule dynamics rather than cargo transporters. The weakly bound slip state, reminiscent of a molecular safety leash, may be an adaptation for high processivity.
DO - 10.1016/j.bpj.2013.02.040
UR - http://www.dx.doi.org/10.1016/j.bpj.2013.02.040
ER -