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

Autor: Meier SM; Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.; Department of Biology, Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.; Bringing Materials to Life Initiative, ETH Zürich, Zürich, Switzerland., Farcas AM; Department of Biology, Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.; Bringing Materials to Life Initiative, ETH Zürich, Zürich, Switzerland., Kumar A; Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland.; ImmunOs Therapeutics AG, Schlieren, Switzerland., Ijavi M; Bringing Materials to Life Initiative, ETH Zürich, Zürich, Switzerland.; Department of Materials, ETH Zürich, Zürich, Switzerland., Bill RT; Department of Biology, Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.; Department of Molecular Life Sciences, University of Zürich, Zürich, Switzerland., Stelling J; Department of Biosystems Science and Engineering and SIB Swiss Institute of Bioinformatics, ETH Zürich, Basel, Switzerland., Dufresne ER; Bringing Materials to Life Initiative, ETH Zürich, Zürich, Switzerland.; Department of Materials, ETH Zürich, Zürich, Switzerland., Steinmetz MO; Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen, Switzerland. michel.steinmetz@psi.ch.; University of Basel, Biozentrum, Basel, Switzerland. michel.steinmetz@psi.ch., Barral Y; Department of Biology, Institute of Biochemistry, ETH Zürich, Zürich, Switzerland. yves.barral@bc.biol.ethz.ch.; Bringing Materials to Life Initiative, ETH Zürich, Zürich, Switzerland. yves.barral@bc.biol.ethz.ch.
Jazyk: angličtina
Zdroj: Nature cell biology [Nat Cell Biol] 2023 Jan; Vol. 25 (1), pp. 56-67. Date of Electronic Publication: 2022 Dec 19.
DOI: 10.1038/s41556-022-01035-2
Abstrakt: 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.
(© 2022. The Author(s).)
Databáze: MEDLINE
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