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

Cornell Affiliated Author(s)

Author

S.M. Meier
A.-M. Farcas
A. Kumar
M. Ijavi
R.T. Bill
J. Stelling
E.R. Dufresne
M.O. Steinmetz
Y. Barral

Abstract

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).

Date Published

Journal

Nature Cell Biology

Volume

25

Issue

1

Number of Pages

56-67,

ISBN Number

14657392 (ISSN)

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85144191692&doi=10.1038%2fs41556-022-01035-2&partnerID=40&md5=4048f61522cec8f2742abb7b1e0b7524

DOI

10.1038/s41556-022-01035-2

Alternate Journal

Nat. Cell Biol.

Group (Lab)

Eric Dufresne Group

Funding Source

2012/192 TubeX
310030_192566
31003A-105904
31003A_166608
CRSII5_189940

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