Force-velocity relationships in kinesin-driven motility

Kirsten Hall, Douglas G. Cole, Yin Yeh, Jonathan M. Scholey, Ronald J. Baskin

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

KINESIN is a microtubule-based motor protein that uses energy released from Mg-ATP hydrolysis to generate force for the movement of intracellular membranes towards the fast-growing (plus) ends of microtubule tracks in cells1. Kinesin-driven microtubule movement can be visualized and quantified using light microscope motility assays2-5 but our understanding of how kinesin generates force and motion is incomplete6. Here we report the use of a centrifuge microscope7,8 to obtain force-velocity curves for kinesin-driven motility and to estimate that the maximal isometric force generated per kinesin is 0.12 ± 0.03 pN per molecule.

Original languageEnglish (US)
Pages (from-to)457-459
Number of pages3
JournalNature
Volume364
Issue number6436
StatePublished - Jul 29 1993

Fingerprint

Kinesin
Microtubules
Intracellular Membranes
Hydrolysis
Adenosine Triphosphate
Light
Proteins

ASJC Scopus subject areas

  • General

Cite this

Hall, K., Cole, D. G., Yeh, Y., Scholey, J. M., & Baskin, R. J. (1993). Force-velocity relationships in kinesin-driven motility. Nature, 364(6436), 457-459.

Force-velocity relationships in kinesin-driven motility. / Hall, Kirsten; Cole, Douglas G.; Yeh, Yin; Scholey, Jonathan M.; Baskin, Ronald J.

In: Nature, Vol. 364, No. 6436, 29.07.1993, p. 457-459.

Research output: Contribution to journalArticle

Hall, K, Cole, DG, Yeh, Y, Scholey, JM & Baskin, RJ 1993, 'Force-velocity relationships in kinesin-driven motility', Nature, vol. 364, no. 6436, pp. 457-459.
Hall K, Cole DG, Yeh Y, Scholey JM, Baskin RJ. Force-velocity relationships in kinesin-driven motility. Nature. 1993 Jul 29;364(6436):457-459.
Hall, Kirsten ; Cole, Douglas G. ; Yeh, Yin ; Scholey, Jonathan M. ; Baskin, Ronald J. / Force-velocity relationships in kinesin-driven motility. In: Nature. 1993 ; Vol. 364, No. 6436. pp. 457-459.
@article{20697c26cea54c83b6acf5243252b923,
title = "Force-velocity relationships in kinesin-driven motility",
abstract = "KINESIN is a microtubule-based motor protein that uses energy released from Mg-ATP hydrolysis to generate force for the movement of intracellular membranes towards the fast-growing (plus) ends of microtubule tracks in cells1. Kinesin-driven microtubule movement can be visualized and quantified using light microscope motility assays2-5 but our understanding of how kinesin generates force and motion is incomplete6. Here we report the use of a centrifuge microscope7,8 to obtain force-velocity curves for kinesin-driven motility and to estimate that the maximal isometric force generated per kinesin is 0.12 ± 0.03 pN per molecule.",
author = "Kirsten Hall and Cole, {Douglas G.} and Yin Yeh and Scholey, {Jonathan M.} and Baskin, {Ronald J.}",
year = "1993",
month = "7",
day = "29",
language = "English (US)",
volume = "364",
pages = "457--459",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6436",

}

TY - JOUR

T1 - Force-velocity relationships in kinesin-driven motility

AU - Hall, Kirsten

AU - Cole, Douglas G.

AU - Yeh, Yin

AU - Scholey, Jonathan M.

AU - Baskin, Ronald J.

PY - 1993/7/29

Y1 - 1993/7/29

N2 - KINESIN is a microtubule-based motor protein that uses energy released from Mg-ATP hydrolysis to generate force for the movement of intracellular membranes towards the fast-growing (plus) ends of microtubule tracks in cells1. Kinesin-driven microtubule movement can be visualized and quantified using light microscope motility assays2-5 but our understanding of how kinesin generates force and motion is incomplete6. Here we report the use of a centrifuge microscope7,8 to obtain force-velocity curves for kinesin-driven motility and to estimate that the maximal isometric force generated per kinesin is 0.12 ± 0.03 pN per molecule.

AB - KINESIN is a microtubule-based motor protein that uses energy released from Mg-ATP hydrolysis to generate force for the movement of intracellular membranes towards the fast-growing (plus) ends of microtubule tracks in cells1. Kinesin-driven microtubule movement can be visualized and quantified using light microscope motility assays2-5 but our understanding of how kinesin generates force and motion is incomplete6. Here we report the use of a centrifuge microscope7,8 to obtain force-velocity curves for kinesin-driven motility and to estimate that the maximal isometric force generated per kinesin is 0.12 ± 0.03 pN per molecule.

UR - http://www.scopus.com/inward/record.url?scp=0027224127&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027224127&partnerID=8YFLogxK

M3 - Article

VL - 364

SP - 457

EP - 459

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6436

ER -