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Phase separation

+TIPs condense on microtubule plus-ends

Nature Cell Biology volume 25, pages 12–14 (2023)Cite this article

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End-binding proteins attach to the dynamic plus-ends of microtubules in order to regulate microtubule polymerization and the transport of other plus-end tracking proteins (+TIPs). Three new studies dissect the multivalent interactions that constitute distinct +TIP networks and reveal that they give rise to liquid-like biomolecular condensates.

In these three papers, the authors establish that the interactions required to form functional +TIP networks are densely multivalent, highly redundant, and of moderate affinity. Although this was already appreciated5, these studies link such interactions to the physical properties of +TIP networks. That is, the authors all identified their +TIP networks of study as liquid-like biomolecular condensates6, joining a growing list of cytoskeletal condensates7. It is particularly exciting that +TIPs display this behaviour, as the cohesive yet dynamic mechanical properties of condensates lend themselves well to regulate the growing and shrinking microtubule plus-end, as we will explain in the examples below.

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Fig. 1: Condensates of plus-end tracking proteins on microtubules.

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Authors and Affiliations

  1. Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA

    Bernardo Gouveia

  2. Department of Molecular Biology, Princeton University, Princeton, NJ, USA

    Sabine Petry

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  1. Bernardo Gouveia
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  2. Sabine Petry
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Correspondence to Sabine Petry.

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Gouveia, B., Petry, S. +TIPs condense on microtubule plus-ends. Nat Cell Biol 25, 12–14 (2023). https://doi.org/10.1038/s41556-022-01068-7

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