Structural basis for lamin assembly at the molecular level

Jinsook Ahn, Inseong Jo, So-mi Kang, Seokho Hong, Suhyeon Kim, Soyeon Jeong, Yong-Hak Kim, Bum-Joon Park and Nam-Chul Ha ()
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Jinsook Ahn: Seoul National University
Inseong Jo: Seoul National University
So-mi Kang: Pusan National University
Seokho Hong: Seoul National University
Suhyeon Kim: Seoul National University
Soyeon Jeong: Seoul National University
Yong-Hak Kim: Catholic University of Daegu School of Medicine
Bum-Joon Park: Pusan National University
Nam-Chul Ha: Seoul National University

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-11684-x

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