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BP: Fachverband Biologische Physik

BP 26: From Single-Molecule to Tissue Dynamics

BP 26.4: Vortrag

Donnerstag, 25. März 2010, 15:00–15:15, H43

Cooperative binding of kinesin motors on microtubules studied with atomic force microscopy — •Karen Hollenberg, Iwan A. T. Schaap, and Christoph F. Schmidt — Drittes Physikalisches Institut, Fakultät für Physik, Georg-August-Universität Göttingen

Kinesin motor proteins move actively along microtubules and drive intracellular transport of vesicles and organelles in cells. Since most transport processes involve smaller or larger ensembles of motors, it is an interesting question if and how motors communicate and coordinate their activity in such ensembles. One possibility is direct head-to-head interaction. An intriguing alternative is interaction via the substrate, the microtubule lattice.

We have here used atomic force microscopy in buffer to search for axial and lateral cooperativity in the binding of motors. The results show that kinesin-1 dimers and monomers cluster when immobilized on the track by AMP-PNP. For monomers this effect is less pronounced.