Structural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance.

ABSTRACT: SSNA-1 is a fibrillar protein localized at the area where dynamic microtubule remodeling occurs including centrosomes. Despite the important activities of SSNA1 to microtubules such as nucleation, co-polymerization, and lattice sharing microtubule branching, the underlying molecular mechanism have remained unclear due to a lack of structural information. Here, we determined the cryo-EM structure of C. elegans SSNA-1 at 4.55 Å resolution and evaluated its role during embryonic development in C. elegans. We found that SSNA1 forms an anti-parallel coiled-coil, and its self-assembly is facilitated by the overhangs of 16 residues at its C-terminus, which dock on the adjacent coiled-coil to form a triple-stranded helical junction. Notably, the microtubule-binding region is within t

SUBMITTER: Agostini L 

PROVIDER: S-EPMC11722292 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature