CAMSAP2 organizes a gamma-tubulin-independent microtubule nucleation centre through phase separation

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抄録

Microtubules are dynamic polymers consisting of αβ-tubulin heterodimers. The initial polymerization process, called microtubule nucleation, occurs spontaneously via αβ-tubulin. Since a large energy barrier prevents microtubule nucleation in cells, the γ-tubulin ring complex is recruited to the centrosome to overcome the nucleation barrier. However, a considerable number of microtubules can polymerize independently of the centrosome in various cell types. Here, we present evidence that the minus-end-binding calmodulin-regulated spectrin-associated protein 2 (CAMSAP2) serves as a strong nucleator for microtubule formation by significantly reducing the nucleation barrier. CAMSAP2 co-condensates with αβ-tubulin via a phase separation process, producing plenty of nucleation intermediates. Microtubules then radiate from the co-condensates, resulting in aster-like structure formation. CAMSAP2 localizes at the co-condensates and decorates the radiating microtubule lattices to some extent. Taken together, these in vitro findings suggest that CAMSAP2 supports microtubule nucleation and growth by organizing a nucleation centre as well as by stabilizing microtubule intermediates and growing microtubules.

収録刊行物

  • eLife

    eLife 11 e77365-, 2022-06-28

    eLife Sciences Publications

キーワード

詳細情報 詳細情報について

  • CRID
    1050294045367927552
  • ISSN
    2050084X
  • HANDLE
    20.500.14094/90009483
  • 本文言語コード
    en
  • 資料種別
    journal article
  • データソース種別
    • IRDB

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