Arabidopsis CaLB1 undergoes phase separation with the ESCRT protein ALIX and modulates autophagosome maturation

Niccolò Mosesso, Niharika Savant Lerner, Tobias Bläske, Felix Groh, Shane Maguire, Marie Laura Niedermeier, Eliane Landwehr, Karin Vogel, Konstanze Meergans, Marie-Kristin Nagel, Malte Drescher, Florian Stengel, Karin Hauser and Erika Isono ()
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Niccolò Mosesso: University of Konstanz
Niharika Savant Lerner: University of Konstanz
Tobias Bläske: University of Konstanz
Felix Groh: University of Konstanz
Shane Maguire: University of Konstanz
Marie Laura Niedermeier: University of Konstanz
Eliane Landwehr: University of Konstanz
Karin Vogel: University of Konstanz
Konstanze Meergans: University of Konstanz
Marie-Kristin Nagel: University of Konstanz
Malte Drescher: University of Konstanz
Florian Stengel: University of Konstanz
Karin Hauser: University of Konstanz
Erika Isono: University of Konstanz

Nature Communications, 2024, vol. 15, issue 1, 1-20

Abstract: Abstract Autophagy is relevant for diverse processes in eukaryotic cells, making its regulation of fundamental importance. The formation and maturation of autophagosomes require a complex choreography of numerous factors. The endosomal sorting complex required for transport (ESCRT) is implicated in the final step of autophagosomal maturation by sealing of the phagophore membrane. ESCRT-III components were shown to mediate membrane scission by forming filaments that interact with cellular membranes. However, the molecular mechanisms underlying the recruitment of ESCRTs to non-endosomal membranes remain largely unknown. Here we focus on the ESCRT-associated protein ALG2-interacting protein X (ALIX) and identify Ca2+-dependent lipid binding protein 1 (CaLB1) as its interactor. Our findings demonstrate that CaLB1 interacts with AUTOPHAGY8 (ATG8) and PI(3)P, a phospholipid found in autophagosomal membranes. Moreover, CaLB1 and ALIX localize with ATG8 on autophagosomes upon salt treatment and assemble together into condensates. The depletion of CaLB1 impacts the maturation of salt-induced autophagosomes and leads to reduced delivery of autophagosomes to the vacuole. Here, we propose a crucial role of CaLB1 in augmenting phase separation of ALIX, facilitating the recruitment of ESCRT-III to the site of phagophore closure thereby ensuring efficient maturation of autophagosomes.

Date: 2024
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DOI: 10.1038/s41467-024-49485-6

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