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. 2018 Sep 7;9:1277. doi: 10.3389/fphys.2018.01277

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Copyright © 2018 Janin and Gache.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Nesprins and lamins as part of the LINC complex. (A) Nesprins and lamins isoforms structures. AD, adaptive domain; EBD, emerin binding domain; KASH domain, Klarsicht/ANC-1/Syne Homology; LBD, lamin binding domain; NBD, nesprin binding domain; SR, spectrin repeats. (B) The healthy LINC complex and its interactors. Nesprins play multiple functions at ONM but also at INM. Full-length nesprins take part at the ONM to the bridge linking the nucleus to the actin cytoskeleton and shorter isoforms, such as nesprin-1a, interact via Akap450 and KLC-1/2 with microtubules. At the same time, smaller isoforms interact with the nucleoskeleton at INM. (C) When a mutation affects LMNA or SYNE genes, the disruption of the LINC complex participates to the physiopathogenesis of the diseases by structural defects, nuclear migration and anchoring defects and cell signaling pathways and gene expression regulation defects. NE, nuclear envelope; LINC, linker of nucleoskeleton to cytoskeleton; ONM, outer nuclear membrane; INM, inner nuclear membrane; KASH domain, Klarsicht/ANC-1/Syne homology; SUN, Sad1p/UNC84; BAF, barrier to auto-integration factor.