Nonprocessive motor dynamics at the microtubule membrane tube interface.
Key cellular processes such as cell division, membrane compartmentalization, and intracellular transport rely on motor proteins. Motors have been studied in detail on the single motor level such that information on their step size, stall force, average run length, and processivity are well known. However, in vivo, motors often work together, so that the question of their collective coordination has raised great interest. Here, we specifically attach motors to giant vesicles and examine collective motor dynamics during membrane tube formation. Image correlation spectroscopy reveals directed motion as processive motors walk at typical speeds (< or = 500 nm/s) along an underlying microtubule and accumulate at the tip of the growing membrane tube. In contrast, nonprocessive motors exhibit purely diffusive behavior, decorating the entire length of a microtubule lattice with diffusion constants at least 1000 times smaller than a freely-diffusing lipid-motor complex in a lipid bilayer (1 microm(2)/s); fluorescence recovery after photobleaching experiments confirm the presence of the slower-moving motor population at the microtubule-membrane tube interface. We suggest that nonprocessive motors dynamically bind and unbind to maintain a continuous interaction with the microtubule. This dynamic and continuous interaction is likely necessary for nonprocessive motors to mediate bidirectional membrane tube dynamics reported previously.
Shaklee
Paige M
PM
Physics of Life Processes, Leiden Institute of Physics, Leiden University, Leiden, The Netherlands. p.shaklee@amolf.nl
Bourel-Bonnet
Line
L
Dogterom
Marileen
M
Schmidt
Thomas
T
D002462:Cell Membrane / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D007700:Kinetics; D008870:Microtubules / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation
D020409:Molecular Motor Proteins