Myosin V processivity: Multiple kinetic pathways for head-to-head coordination
- 31 March 2004
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 101 (15) , 5542-5546
- https://doi.org/10.1073/pnas.0307247101
Abstract
Myosin V, a double-headed molecular motor, transports organelles within cells by walking processively along actin, a process that requires coordination between the heads. To understand the mechanism underlying this coordination, processive runs of single myosin V molecules were perturbed by varying nucleotide content. Contrary to current views, our results show that the two heads of a myosin V molecule communicate, not through any one mechanism but through an elaborate system of cooperative mechanisms involving multiple kinetic pathways. These mechanisms introduce redundancy and safeguards that ensure robust processivity under differing physiologic demands.Keywords
This publication has 32 references indexed in Scilit:
- Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezersNature Cell Biology, 2003
- The Unique Properties of Tonic Smooth Muscle Emerge from Intrinsic as Well as Intermolecular Behaviors of Myosin MoleculesJournal of Biological Chemistry, 2003
- Myosin V Walks Hand-Over-Hand: Single Fluorophore Imaging with 1.5-nm LocalizationScience, 2003
- Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarizationNature, 2003
- The motor domain determines the large step of myosin-VNature, 2002
- Kinetic Mechanism and Regulation of Myosin VIJournal of Biological Chemistry, 2001
- Interaction of Actin and ADP with the Head Domain of Smooth Muscle Myosin: Implications for Strain-Dependent ADP Release in Smooth MuscleBiochemistry, 1998
- ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosinNature Structural & Molecular Biology, 1996
- A 35-Å movement of smooth muscle myosin on ADP releaseNature, 1995
- Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro.The Journal of cell biology, 1990