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

• Type: Article in International Scientific Journal
• Date: 2023

Authors

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

Journal

Title: Science advances

Vol. 9

Publisher: American Association for the Advancement of Science

Indexing

ISI Web of Knowledge - 0 Citations

Scopus

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 19