Evaluation of Kinesin Head-Microtubule Binding Stability Changes Influenced by Microtubule-Binding Molecules

We describe kinesin head (KH)-microtubule (MT) interaction changes influenced by MT-binding molecules, revealed by single-molecule force spectroscopy. KH-MT interactions in the absence of nucleotides and in the presence of ATP and ADP were evaluated by rupture force measurements using atomic force microscopy. These measurements were used for monitoring interaction changes by the MT-stabilizing/destabilizing factors including paclitaxel concentration change, nocodazole, and colchicine treatment. Average rupture forces of KH-MT at low paclitaxel concentration and nocodazole treatment were decreased by approximately 10 pN compared with normal KH-MT. This report describes KH-MT interaction changes resulting from MT-binding molecules as well as basic information for the understating of kinesin motility along MT.