Regensburg 2019 – scientific programme
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BP: Fachverband Biologische Physik
BP 6: Poster I
BP 6.9: Poster
Monday, April 1, 2019, 17:30–19:30, Poster B2
MT-kinesin bundle and cross-linked network formation — •Amna Abdalla Mohammed Khalid1, Fanomezana Moutse Ranaivoson2, Anne Houdusse2, and Christoph F. Schmidt1,3 — 1Drittes Physikalisches Institut - Biophysik, Fakultät für Physik, Georg-August-Universität, Göttingen, Germany. — 2Structural Motility Group, Institut Curie, Paris, France — 3Department of Physics, Duke University, Durham, USA
The mitotic kinesin-like protein 2 (MKLP2), is an N-terminal kinesin of the kinesin 6 family. MKLP2 plays critical roles in mitosis, in particular for the metaphase to anaphase transition and for cytokinesis. This kinesin motor is likely to have a diverging mechanism due to several inserts near the motor domain and the neck-linker which make the motor domain ∼ 60% larger than that of other kinesins. Its neck-linker is four times longer than that found in other kinesins. We studied dimeric truncated MKLP2 in vitro motility experiments. It is an active motor, although we have not found any processive motility yet in single-molecule assays. A conspicuous feature of this kinesin is its high microtubule (MT) bundling activity. MKLP2 has the ability to form 2D and 3D strongly bundled cross-linked MT networks that evolve and coarsen slowly in time over many hours. We hypothesize that these bundled networks are occurring as a collective dynamic phenomenon based on weak and reversible interactions between the motors and the microtubules.