Dresden 2017 – scientific programme

Parts | Days | Selection | Search | Updates | Downloads | Help

BP: Fachverband Biologische Physik

BP 5: Single Molecule Biophysics

BP 5.9: Talk

Monday, March 20, 2017, 17:15–17:30, HÜL 386

In vitro study of the regulation and the mechanism of the MKLp2 mitotic kinesin — •Amna Abdalla Mohammed Khalid¹, I-Mei Yu², Christoph Schmidt¹, and Anne Houdusse² — ¹Third Institute of Physics - Biophysics, Georg August University, Germany — ²Institut Curie Paris, France

The mitotic kinesin-like protein 2 (MKLp2), is a N-terminal kinesin of the Kinesin-6 family with unique features. It plays critical roles for the metaphase to anaphase transition and for cytokinesis in cell division. Previous studies have shown that MKlp2 inhibitors reduced the cell growth in pancreatic adenocarcinoma cells and can kill tumour stem cells. On the other hand, MKlp2 is overexpressed in variety of cancers. Therefore it is considered as a good candidate for new cancer therapies. High-resolution single-molecule studies are fundamental to understand the regulation and mechanism of MKlp2 at the molecular level. We are studying truncated MKLp2 constructs to explore basic motor functions and to understand the influence the domains on motor properties. Here I present single-molecule studies of a dimeric truncated MKlp2, in vitro using total internal reflection fluorescence microscopy (TIRFM). Our data confirm that the dimeric truncated MKlp2 motors are active. A conspicuous feature of this motor is its microtubule bundling activity.