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. 2020 Jan 1;219(2):e201908182. doi: 10.1083/jcb.201908182

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© 2020 Chen et al.

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 6. — A model describing how RTN3 and RTN4 protect ER membrane integrity during ER escape of macromolecular protein complexes. Top: During ER exit of SV40 into the cytosol, a decisive infection step, both RTN3 and RTN4 are recruited to the ER focus. The RTN proteins are thought to provide flexibility to the ER membrane by inducing ER membrane curvature at the ER focus. This activity protects the fidelity of the ER membrane when the viral particles penetrate this barrier. Bottom: During ER exit of aggregated Akita (A), RTN3 is recruited to a site that initiates ER-phagy. Similar to SV40, we propose that RTN3 imparts flexibility to the ER membrane by triggering ER membrane curvature at the ER exit site. Once the Akita aggregates exit the ER, it is targeted to the lysosome for degradation.