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88 reviewsSUMMARYAutophagosomes originate from and maintain association with the endoplasmic reticulum (ER) during theirformation, yet how these processes are molecularly coordinated in plants remains poorly understood. Here,we demonstrate that Arabidopsis autophagy-related protein 18a (ATG18a), a key organizer of early autophagosome formation, undergoes phase separation to form biomolecular condensates on the ER membrane,which progress from highly mobile droplets to stable ring-like structures, while the ER is reshaped. Wediscovered that ATG18a condensates work together with ROOT HAIR DEFECTIVE3 (RHD3), an ER membrane-shaping protein, with RABC1 serving as a molecular linker between them. Importantly, RABC1 facilitates both RHD3 assembly necessary for the formation of ring-like ER structures and its interaction withATG18a condensates. These findings reveal a mechanism whereby biomolecular condensates work togetherwith membrane-shaping proteins to reshape specialized membrane domains through wetting interactions,providing an insight into autophagosome formation in plant stress responses.
