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. 2017 Mar 6;216(3):543–545. doi: 10.1083/jcb.201701054

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© 2017 Starr and Rose

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

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Figure 1. — TAN lines. TAN lines include LINC complexes made of the inner nuclear membrane (INM) protein Sun2 and the outer nuclear membrane (ONM) protein nesprin-2. LINC complexes connect to lamins and other INM proteins, including Samp1. Nesprin-2 mediates interactions with actin cables through its calponin homology (CH) domains, FHOD1 and Fascin. TorsinA and LAP1 form a heterocomplex at the INM; arrows and question marks indicate their possible targets. (left) TorsinA/LAP1 could mediate LINC complex formation by freeing nesprin-2 to associate in TAN lines or allowing Sun2 monomers to form trimers. (right) TorsinA/LAP1 could function through unknown targets independently of the LINC to regulate actin assembly.