Loading direction regulates the affinity of ADP for kinesin

• Published in: Nature structural & molecular biology Vol. 10; no. 4; pp. 308 - 311
• Main Authors: Ishiwata, Shin'ichi, Uemura, Sotaro
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.04.2003
• Subjects: Adenosine Diphosphate - metabolism; Animals; Biophysical Phenomena; Biophysics; Cattle; In Vitro Techniques; Kinesin - chemistry; Kinesin - metabolism; Kinetics; Microtubules - metabolism; Models, Biological; Molecular Motor Proteins - chemistry; Molecular Motor Proteins - metabolism; Sus scrofa
• ISSN: 1072-8368; 1545-9993; 2331-365X; 1545-9985
• DOI: 10.1038/nsb911

Kinesin is an ATP-driven molecular motor that moves processively along a microtubule. Processivity has been explained as a mechanism that involves alternating single- and double-headed binding of kinesin to microtubules coupled to the ATPase cycle of the motor. The internal load imposed between the two bound heads has been proposed to be a key factor regulating the ATPase cycle in each head. Here we show that external load imposed along the direction of motility on a single kinesin molecule enhances the binding affinity of ADP for kinesin, whereas an external load imposed against the direction of motility decreases it. This coupling between loading direction and enzymatic activity is in accord with the idea that the internal load plays a key role in the unidirectional and cooperative movement of processive motors.