2008/01/18 by Ram Dixit, Jennifer L. Ross, Yale E. Goldman +1 · 2 citations
Biochemistry, Genetics and Molecular Biology · #Microtubule and mitosis dynamics #Cellular transport and secretion #Photosynthetic Processes and Mechanisms
paper · doi:10.1126/science.1152993
openalex publication_date 2008/01/18 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Dynein and kinesin motor proteins transport cellular cargoes toward opposite ends of microtubule tracks. In neurons, microtubules are abundantly decorated with microtubule-associated proteins (MAPs) such as tau. Motor proteins thus encounter MAPs frequently along their path. To determine the effects of tau on dynein and kinesin motility, we conducted single-molecule studies of motor proteins moving along tau-decorated microtubules. Dynein tended to reverse direction, whereas kinesin tended to detach at patches of bound tau. Kinesin was inhibited at about a tenth of the tau concentration that inhibited dynein, and the microtubule-binding domain of tau was sufficient to inhibit motor activity. The differential modulation of dynein and kinesin motility suggests that MAPs can spatially regulate the balance of microtubule-dependent axonal transport.