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Load-dependent ADP binding to myosins V and VI: implications for subunit coordination and function.

Yusuke Oguchi¹, Sergey V Mikhailenko, Takashi Ohki

¹Department of Physics, Faculty of Science and Engineering, Waseda University, Tokyo 169-8555, Japan.

Proceedings of the National Academy of Sciences of the United States of America

|May 30, 2008

Summary

External loads alter how quickly ADP binds to myosin V and VI motors, influencing their movement direction and cellular roles. This load-dependent binding is key to their distinct functions.

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Area of Science:

Molecular biology
Cellular mechanics
Biophysics

Background:

Dimeric myosins V and VI are motor proteins that move along actin filaments.
Their movement is a "hand-over-hand" process, crucial for cellular transport.
ADP dissociation is a rate-limiting step in their catalytic cycle.

Purpose of the Study:

To investigate how external loads affect ADP binding affinity in myosins V and VI.
To understand the role of load-dependent kinetics in myosin motor function.

Main Methods:

Applying external loads to individual actomyosin V and VI bonds.
Model-based analysis of ADP binding and dissociation kinetics.
Calculating intramolecular loads during processive stepping.

Main Results:

External loads asymmetrically affect ADP binding, weakening it when assisting motility.
Forward loads accelerate ADP dissociation; backward loads inhibit it.
Loads slow ADP binding to myosin V but accelerate it for myosin VI.

Conclusions:

The distinct load dependence of ADP binding kinetics differentiates myosin V and VI functions.
Intramolecular load during stepping is approximately 2 pN for both myosins.
This load sensitivity allows myosins to perform specialized cellular tasks.