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Structural basis for lamin assembly at the molecular level
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Structural basis for lamin assembly at the molecular level
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Journal Article
Structural basis for lamin assembly at the molecular level
2019
Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 101/58
/ 14/19
/ 14/34
/ 140/146
/ 82/80
/ 82/83
/ Assembly
/ Coils
/ Cross-Linking Reagents - chemistry
/ Dimers
/ Helices
/ Humanities and Social Sciences
/ Humans
/ Intermediate Filaments - metabolism
/ Lamins
/ Mutation
/ Nuclear Proteins - chemistry
/ Nuclear Proteins - ultrastructure
/ Peptide Fragments - chemistry
/ Protein Conformation, alpha-Helical
/ Proteins
/ Science
