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Multivalency ensures persistence of a +TIP body at specialized microtubule ends.

Sandro M MeierAna-Maria FarcasAnil KumarMahdiye IjaviRobert T BillJoerg StellingEric R DufresneMichel O SteinmetzYves Barral
Published in: Nature cell biology (2022)
Microtubule plus-end tracking proteins (+TIPs) control microtubule specialization and are as such essential for cell division and morphogenesis. Here we investigated interactions and functions of the budding yeast Kar9 network consisting of the core +TIP proteins Kar9 (functional homologue of APC, MACF and SLAIN), Bim1 (orthologous to EB1) and Bik1 (orthologous to CLIP-170). A multivalent web of redundant interactions links the three +TIPs together to form a '+TIP body' at the end of chosen microtubules. This body behaves as a liquid condensate that allows it to persist on both growing and shrinking microtubule ends, and to function as a mechanical coupling device between microtubules and actin cables. Our study identifies nanometre-scale condensates as effective cellular structures and underlines the power of dissecting the web of low-affinity interactions driving liquid-liquid phase separation in order to establish how condensation processes support cell function.
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