Addressing the Molecular Mechanism of Longitudinal Lamin Assembly Using Chimeric Fusions.

ABSTRACT: The molecular architecture and assembly mechanism of intermediate filaments have been enigmatic for decades. Among those, lamin filaments are of particular interest due to their universal role in cell nucleus and numerous disease-related mutations. Filament assembly is driven by specific interactions of the elementary dimers, which consist of the central coiled-coil rod domain flanked by non-helical head and tail domains. We aimed to investigate the longitudinal 'head-to-tail' interaction of lamin dimers (the so-called A_CN interaction), which is crucial for filament assembly. To this end, we prepared a series of recombinant fragments of human lamin A centred around the N- and C-termini of the rod. The fragments were stabilized by fusions to heterologous capping motifs which prov

SUBMITTER: Stalmans G 

PROVIDER: S-EPMC7407374 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature