Assembly of a nuclear lamin coil 2 fragment

ABSTRACT: Nuclear structure and function are governed by lamins, which are intermediate filaments mostly consisting of α-helices. Different lamin assembly models have been proposed based on low resolution or fragmented structures. However, their assembly mechanisms at the molecular level are poorly understood. The structure shows the anti-parallel arrangement of two coiled-coil dimers, which is important for the assembly process. We further discovered a new interaction of a coil 2 by using chemical cross-linking and mass analysis, of which the results were deposited in the PRIDE identifier PXD013144. Here we showed that a cysteine-substituted coil 2 R388C segment (286-400 amino acid residues of lamin) was dimerized by the chemical crosslinking. Our findings also provide a molecular basis for the assembly mechanisms of other intermediate filaments.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

DISEASE(S): Progeria

SUBMITTER: Yong-Hak Kim  

LAB HEAD: Yong-Hak Kim

PROVIDER: PXD014029 | Pride | 2025-12-15

REPOSITORIES: Pride