Endoplasmic reticulum exit sites (ERESs) are ER subdomains where coat protein complex II carriers are assembled for ER-to-Golgi transport. We previously proposed a dynamic capture-and-release model of ERESs by Golgi stacks in plants. However, how ERESs and Golgi stacks maintain a stable interaction in plant cells with vigorous cytoplasmic streaming is unknown. Here, we show that a plant-specific ER transmembrane protein, which we designate as MAG3, plays a crucial role in mediating the capture-and-release of ERESs in Arabidopsis. We isolated a mutant (mag3) defective in protein exit from the ER in seeds. MAG3 localized specifically to the ER-Golgi interface with Golgi-associated ERESs and remained there after ERES release. MAG3 deficiency caused a reduction in the amount of ERESs associated with each Golgi stack. MAG3 interacted with WPP DOMAIN PROTEINs, which are also plant-specific. These results suggest that plants have evolved a unique system to support ER-to-Golgi transport despite intracellular motility.
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| http://dx.doi.org/10.1038/s42003-025-07602-1 | DOI Listing |
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Article Synopsis
- Plant cells struggle with efficiently moving proteins from the endoplasmic reticulum (ER) to the Golgi apparatus, and the study focuses on a protein transport mutant in Arabidopsis thaliana called mag5.
- The mag5 mutant accumulates storage protein precursors in seeds and has a deletion in the gene related to a crucial component (Sec16) for proper ER export.
- The findings show that the MAG5 protein is important for regulating the COPII coat's association with ER exit sites, impacting how proteins are exported to the Golgi, indicating its vital role in plant cell cargo transport.
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