ArticleScience advances2026
RanGAP1 coordinates the ER-lamina interface to drive de novo nuclear envelope reassembly in mouse embryos.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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10 authors.
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Abstract
Nuclear envelope (NE) reassembly is essential for the zygote-to-totipotency transition in mammalian embryos. Beyond its classical roles in nuclear transport and maintenance of the RanGTP gradient, the function of RanGAP1 in embryonic NE reassembly has remained elusive. Here, we show that RanGAP1 localizes to the early embryonic NE, driving reassembly via a distinct structural mechanism. Trim-Away-mediated RanGAP1 depletion causes two-cell stage arrest and severe NE defects, including nuclear pore complex (NPC) loss, failed reassembly, and aberrant "fishnet" membrane structures. Mechanistically, RanGAP1 establishes a structural paradigm for endoplasmic reticulum (ER)-lamina coupling by recruiting Lamin A/C, B1, and B2 to the ER for coassembly. The acidic domain and SUMO-1 modification at Lys
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