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. 2022 Aug 8;221(9):e202112068. doi: 10.1083/jcb.202112068

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© 2022 Renne et al.

This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

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Figure 8. — Model of Seipin enriching NLs via interactions between the hydrophobic helix and NL carboxyl esters. A model for Seipin-mediated packaging of structurally distinct NLs (TAG, pink; SE, green; RE, orange) into LDs. Seipin luminal domain (PDB accession no. 6DS5, visualized using Illustrate [Goodsell et al., 2019]) protrudes deeply into the ER membrane, positioning its hydroxyl-containing residues far away from PLs carboxyl esters (black circles) and proximal to the bilayer normal, a position that favors its interaction with NLs carboxyl esters (pink, green, and orange circles on TAG, SE, and RE, respectively). This interaction results in NL enrichment and nucleation within the Seipin ring. Arrows indicate the positions of TMs of the outer Seipin protomers.