CLASP-mediated competitive binding in protein condensates directs microtubule growth

CLASP-mediated competitive binding in protein condensates directs microtubule growth

Blog Article

Abstract Microtubule organization in cells relies on targeting mechanisms.Cytoplasmic linker proteins (CLIPs) and CLIP-associated proteins (CLASPs) are key regulators of microtubule organization, yet the underlying mechanisms remain elusive.Here, we reveal that the C-terminal domain of CLASP2 interacts with a common motif found in several CLASP-binding proteins.

This interaction drives the dynamic localization of CLASP2 to distinct cellular compartments, where retail-packaged CLASP2 accumulates in protein condensates at the cell cortex or the microtubule plus end.These condensates physically contact each other via CLASP2-mediated competitive binding, determining cortical microtubule targeting.The phosphorylation of CLASP2 modulates the dynamics of the condensate-condensate 5 Piece Full Panel Bedroom interaction and spatiotemporally navigates microtubule growth.

Moreover, we identify additional CLASP-interacting proteins that are involved in condensate contacts in a CLASP2-dependent manner, uncovering a general mechanism governing microtubule targeting.Our findings not only unveil a tunable multiphase system regulating microtubule organization, but also offer general mechanistic insights into intricate protein-protein interactions at the mesoscale level.