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PMID: 8332217 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Force-velocity relationships in kinesin-driven motility.

Nature ·Vol. 364 ·No. 6436 ·1993-07-29 ·Pages 457-9

Hall K, Cole DG, Yeh Y, Scholey JM, Baskin RJ

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 cells. Kinesin-driven microtubule movement can be visualized and quantified using light microscope motility assays but our understanding of how kinesin generates force and motion is incomplete. Here we report the use of a centrifuge microscope 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.

MeSH Terms
Adenosine Triphosphate/physiology Animals Biomechanical Phenomena In Vitro Techniques Kinesins/physiology Male Microtubules/physiology Movement/physiology Sea Urchins Sperm Motility/physiology
Chemicals
Adenosine Triphosphate Kinesins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hall K
Section of Molecular and Cellular Biology, University of California, Davis 95616.
Cole D G
Yeh Y
Scholey J M
Baskin R J
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1993-07-29
Pages
457-9
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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