FREE1 regulates phagophore closure in plants
Ying Zhu1,2, Yonglun Zeng1,2, Liwen Jiang3,4,5
1State Key Laboratory of Plant Diversity and Specialty Crops and Guangdong Provincial Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China.
Abstract:
Adenosine monophosphate-activated protein kinase (AMPK), the central energy sensor in more complex eukaryotes, can activate macroautophagy/autophagy upon cellular energy deficiency. However, the regulatory role of nutrient sensing in mediating phagophore closure to generate an autophagosome remains unknown. The evolutionarily conserved endosomal sorting complexes required for transport (ESCRT) machinery has been postulated to regulate phagophore sealing, yet the signaling pathway modulating the ESCRT complex relocation from multivesicular body (MVB) to phagophore for closure remains unknown. We recently identified a plant unique pleiotropic protein FREE1 (FYVE DOMAIN PROTEIN REQUIRED FOR ENDOSOMAL SORTING 1), which is phosphorylated by the plant energy sensor SnRK1 (SNF1-related kinase 1) and bridges the ATG conjugation system and ESCRT machinery to regulate phagophore sealing upon nutrient starvation. This study elucidated the bona fide roles and underlying mechanism of cellular energy-sensing pathways in regulating compartment sealing.
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