Separation of Coiled-Coil Structures in Lamin A/C Is Required for the Elongation of the Filament.

ABSTRACT: Intermediate filaments (IFs) commonly have structural elements of a central α-helical coiled-coil domain consisting of coil 1a, coil 1b, coil 2, and their flanking linkers. Recently, the crystal structure of a long lamin A/C fragment was determined and showed detailed features of a tetrameric unit. The structure further suggested a new binding mode between tetramers, designated eA22, where a parallel overlap of coil 1a and coil 2 is the critical interaction. This study investigated the biochemical effects of genetic mutations causing human diseases, focusing on the eA22 interaction. The mutant proteins exhibited either weakened or augmented interactions between coil 1a and coil 2. The ensuing biochemical results indicated that the interaction requires the separation of the coiled-coils in

SUBMITTER: Ahn J 

PROVIDER: S-EPMC7824274 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature