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BP: Fachverband Biologische Physik
BP 12: Cytoskeleton I
BP 12.2: Vortrag
Dienstag, 10. März 2026, 10:00–10:15, BAR/0205
Mechanical tension extends the microtubule lattice and modulates kinesin-1 binding in an isoform-dependent manner — Yannic Lurz1, Benedikt Fischer1, Laura Muras2, Antoine Rittaud3, Hevré Morhbach4, Igor Kulic3, E. Michael Ostap5, Erik Schaffer1, and •Serapion Pyrpassopoulos1 — 1University of Tübingen — 2University of Uppsala — 3ICS, Strassburg — 4ICPM, Metz — 5University of Pennsylvania
Recent work has shown that the microtubule lattice possesses remarkable structural plasticity, with its conformation modulated by MAPs and motor binding. However, how this plasticity responds to mechanical forces remains poorly understood. We developed assays to measure the effect of tensile forces on single microtubules using optical tweezers and fluorescence microscopy. Decorating microtubules with quantum dots enabled us to measure, with nm-precision, mechanical distortions of ~0.4% under changes in average tensile force <ΔF> = 10.4 pN, within the rage of Fmin = 1.29 pN to Fmax = 20.4 pN, forces comparable to those generated by one to three kinesin-1 motors. Under forces in this range, the average binding rate of KIF5B decreased by ~20%, while its dissociation rate increased by ~10%, reducing its average run length. In extreme cases, run length dropped by up to 46% under tension. By contrast, no statistically significant effects were observed for KIF5C at the same forces. Together, these experiments provide new insights into how microtubules can act as sensors and transducers of mechanical and biochemical cues across the cell.
Keywords: Microtubules; Kinesin; Mechanobiology; Opitcal tweezers; Single-molecule