FINE-TUNING OF KINESINS AND MAPS
Research
Kinesin Regulation
Kinesin-12, KIF15 | Our recent work provided the first biochemical and biophysical characterisation of the tetrameric mitotic kinesin-12, KIF15 (Drechsler et al., eLIFE, 2014 | McHugh et al., MBoC, 2018) and showed that KIF15 motors can cooperate as motor collectives that control microtubule dynamics - i.e., selectively suppress catastrophe events - in a team-size-dependent manner and drive adaptive, geometry-dependent microtubule transport at local microtubule intersections (Drechsler & McAinsh, PNAS, 2016). In combination, KIF15-activities drive the formation of parallel microtubule bundles with synchronized dynamics from a non-ordered array of dynamic microtubules. The discovery of this transport-synchronisation mechanism resolves several apparent conceptual conflicts in the mitosis field and provides an explicit mechanism for KIF15 function during spindle maintenance, which is currently under debate.
Currently, we are investigating the tempo-spatial control of KIF15 during the cell-cycle, trying to functionally dissect multiple cellular subpopulation of this motor using loss-of-function variants of KIF15. For further information on this project, please visit the dedicated project page.
Kinesin-7, Kip2 |Previously, we could show that Kip2, a dimeric kinesin-7 from budding yeast, is phosphorylated by asymmetrically localised homologues of the Glykogen Synthase Kinase 3 (GSK3), triggering the deployment of spindle positioning factors onto astral microtubule plus ends and the bud-cortex (Drechsler et al., JCS, 2015). This study is the first description of GSK3 regulated large-scale microtubule organisation in yeast.
Regulation of Microtubule Associated Proteins
What it takes to become a MAP |In a bottom-up synthetic biology approach, we designed short and simple peptides asking what properties a protein must have to become a microtubule associated protein. Together with the Zhang lab we could demonstrate that already positive charges and multiple microtubule binding interfaces (multivalency) are sufficient to mimick advanced functionality of microtubule associated proteins on (dynamic) micortubules (Drechsler et al., MBoC, 2019).