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

Autor: Sandro M, Meier, Ana-Maria, Farcas, Anil, Kumar, Mahdiye, Ijavi, Robert T, Bill, Jörg, Stelling, Eric R, Dufresne, Michel O, Steinmetz, Yves, Barral
Rok vydání: 2021
Zdroj: Nature cell biology.
ISSN: 1476-4679
Popis: 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.
Databáze: OpenAIRE