CLASP2 recognizes tubulins exposed at the microtubule plus-end in a nucleotide state-sensitive manner

• Tipo: Artigo em Revista Científica Internacional
• Data: 2023

Autores

Luo, WX (Autor) Outra; Demidov, V (Autor) Outra; Shen, Q (Autor) Outra; Girao, H (Autor) Outra; Chakraborty, M (Autor) Outra; Maiorov, A (Autor) Outra; Ataullakhanov, FI (Autor) Outra; Lin, CX (Autor) Outra; Helder Maiato (Autor) FMUP; Grishchuk, EL (Autor) Outra

Revista

Título: Science advances

Vol. 9

Editora: American Association for the Advancement of Science

Indexação

ISI Web of Knowledge - 0 Citações

Scopus

Outras Informações

ID Authenticus: P-00X-PPE

DOI: 10.1126/sciadv.abq5404

Abstract (EN): CLASPs (cytoplasmic linker-associated proteins) are ubiquitous stabilizers of microtubule dynamics, but their molecular targets at the microtubule plus-end are not understood. Using DNA origami-based reconstructions, we show that clusters of human CLASP2 form a load-bearing bond with terminal non-GTP tubulins at the sta-bilized microtubule tip. This activity relies on the unconventional TOG2 domain of CLASP2, which releases its high-affinity bond with non-GTP dimers upon their conversion into polymerization-competent GTP-tubulins. The ability of CLASP2 to recognize nucleotide-specific tubulin conformation and stabilize the catastrophe -pro-moting non-GTP tubulins intertwines with the previously underappreciated exchange between GDP and GTP at terminal tubulins. We propose that TOG2-dependent stabilization of sporadically occurring non-GTP tubulins represents a distinct molecular mechanism to suppress catastrophe at the freely assembling microtubule ends and to promote persistent tubulin assembly at the load-bearing tethered ends, such as at the kinetochores in dividing cells.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 19