Kinesin-1, -2, and -3 motors use family-specific mechanochemical strategies to effectively compete with dynein during bidirectional transport

• DOI: 10.7554/elife.82228
• Publication Date: 2022-09-20T12:03:37Z
• Authors: Allison M Gicking; Tzu-Chen Ma; Qingzhou Feng; Rui Jiang; Somayesadat Badieyan; Michael A Cianfrocco; William O Hancock
• Keywords: Kinesin; Molecular motor

Bidirectional cargo transport in neurons requires competing activity of motors from the kinesin-1, -2, and -3 superfamilies against cytoplasmic dynein-1. Previous studies demonstrated that when kinesin-1 attached to dynein-dynactin-BicD2 (DDB) complex, tethered move slowly with a slight plus-end bias, suggesting overpowers DDB but generates substantial hindering load. Compared kinesin-2 families display higher sensitivity load single-molecule assays are thus predicted be overpowered by dynein complexes transport. To test this prediction, we used DNA scaffold pair members recreate bidirectional vitro, tracked motor pairs using two-channel TIRF microscopy. Unexpectedly, find both kinesin engaged stepping on microtubule, able effectively withstand loads generated DDB. Stochastic simulations reveal compensate for their faster detachment rates under reattachment kinetics. The similar performance between three highlights how kinetics play critical roles balancing forces dynein, emphasizes importance regulation adaptors, regulatory proteins, microtubule track tuning speed directionality cells.