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Meier, S. M.

Publications and source records attributed to Meier, S. M..

2 recordsLinked to original sources

A fluid droplet harvests the force generated by shrinking microtubules in living cells

The energy-consuming dynamic instability of microtubules generates significant forces which are thought to be harnessed to move large cargos in cells. However, identification of mechanisms which can capture the force released during microtubule depolymerization to move large loads has been elusive. In this work we show that a biomolecular condensate provides an elegant solution to this problem. Using live cell super-resolution microscopy, we directly observe that budding yeast +TIP bodies are nanoscale droplets with classic fluid-like behaviors which accumulate type V myosin (Myo2) at their surfaces. We find that conserved self-oligomerization interfaces in the protein Kar9 tune the biophysical properties of the viscoelastic +TIP body and its ability to e]iciently move the mitotic spindle. Our findings introduce a paradigm for how forces generated by microtubule dynamics are harnessed in cells and open a frontier of research on nanoscale biomolecular condensates in their native environment.

biophysics↗

High interaction valency ensures cohesion and persistence of a microtubule +TIP body at the plus-end of a single specialized microtubule in yeast

Microtubule plus-end tracking proteins (+TIPs) control microtubule specialization and are as such essential notably during eukaryotic cell division. Here, we investigated interactions and functions of the budding yeast Kar9 network consisting of the core +TIPs components Kar9 (functional homologue of APC, MACF, and SLAIN), Bim1 (orthologue of EB1), and Bik1 (orthologue of CLIP-170). Our data indicate that a redundant, multivalent web of interactions links the three +TIPs together to form a "Kar9 body" at the tip of a single cytoplasmic microtubule. They further suggest that this body is a liquid-like condensate, allowing it to persist on both growing and shrinking microtubule tips, and functions as a mechanical coupling device between microtubules and actin cables during mitosis. Our study underlines the power of dissecting the web of low-affinity interactions driving liquid-liquid phase separation of proteins in order to demonstrate the importance and establish the functional roles of condensation processes in vivo.

cell biology↗