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- Title
Structural basis for lamin assembly at the molecular level.
- Authors
Ahn, Jinsook; Jo, Inseong; Kang, So-mi; Hong, Seokho; Kim, Suhyeon; Jeong, Soyeon; Kim, Yong-Hak; Park, Bum-Joon; Ha, Nam-Chul
- Abstract
Nuclear structure and function are governed by lamins, which are intermediate filaments that mostly consist of α-helices. Different lamin assembly models have been proposed based on low resolution and fragmented structures. However, their assembly mechanisms are still poorly understood at the molecular level. Here, we present the crystal structure of a long human lamin fragment at 3.2 Å resolution that allows the visualization of the features of the full-length protein. The structure shows an anti-parallel arrangement of the two coiled-coil dimers, which is important for the assembly process. We further discover an interaction between the lamin dimers by using chemical cross-linking and mass spectrometry analysis. Based on these two interactions, we propose a molecular mechanism for lamin assembly that is in agreement with a recent model representing the native state and could explain pathological mutations. Our findings also provide the molecular basis for assembly mechanisms of other intermediate filaments. Lamins are intermediate filaments and the major component of the nuclear lamina. Here the authors determine the crystal structure of a construct comprising the N-terminal half of human lamin A/C and use their structure and cross-linking and biochemical experiments to discuss lamin assembly.
- Subjects
CYTOPLASMIC filaments; MASS analysis (Spectrometry); CHEMICAL ionization mass spectrometry; NUCLEAR structure; LAMINS; CRYSTAL structure
- Publication
Nature Communications, 2019, Vol 10, Issue 1, pN.PAG
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-019-11684-x