A dual phospholipase system instructs membrane hydrolysis during the final stages of plant autophagy
Abstract
Autophagy is a conserved intracellular catabolic process, critical for plant stress tolerance. Upon their delivery in the vacuole, how autophagic bodies containing cargo are hydrolyzed to warrant autophagy degradation remains unclear in multicellular organisms. Here, we found that two Arabidopsis phospholipases, LCAT4 and LCAT3, traffic to the vacuolar lumen and converge on autophagic bodies through fundamentally different routes. While LCAT4 directly binds ATG8 and uses autophagy as a transport system to reach the vacuole prepackaged within autophagosomes, LCAT3 traffics to the lytic compartment independently of autophagosome formation. Knocking out both genes causes an accumulation of autophagic bodies accompanied with a reduction in autophagy degradation. In vivo reconstitution demonstrated that LCAT3 can hydrolyse the membrane of autophagic bodies, enabling the activity of LCAT4 to enhance this process. Together, this work sheds light on the vacuolar stages of autophagy, showing that plants have evolved a multi-component pathway for the efficient disruption of autophagosomal membranes as a critical step for the completion of the autophagy pathway.
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BibTeX
@article{castets2026dual,
title = {{A dual phospholipase system instructs membrane hydrolysis during the final stages of plant autophagy}},
author = {Julie Castets and Matthieu Buridan and Inés Toboso Moreno and Valérie Wattelet-Boyer and Víctor Sánchez de Medina Hernández and Rodrigo Enrique Gomez and Franziska Dittrich-Domergue and Josselin Lupette and Clément Chambaud and Stéphanie Pascal and Tarhan Ibrahim and Tolga O Bozkurt and Yasin Dagdas and Frédéric Domergue and Jérôme Joubès and Elena A Minina and Amélie Bernard},
journal = {Nature Communications},
year = {2026},
month = may,
doi = {10.1038/s41467-026-73116-x},
url = {https://hal.science/hal-05773181v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - A dual phospholipase system instructs membrane hydrolysis during the final stages of plant autophagy
AU - Julie Castets
AU - Matthieu Buridan
AU - Inés Toboso Moreno
AU - Valérie Wattelet-Boyer
AU - Víctor Sánchez de Medina Hernández
AU - Rodrigo Enrique Gomez
AU - Franziska Dittrich-Domergue
AU - Josselin Lupette
AU - Clément Chambaud
AU - Stéphanie Pascal
AU - Tarhan Ibrahim
AU - Tolga O Bozkurt
AU - Yasin Dagdas
AU - Frédéric Domergue
AU - Jérôme Joubès
AU - Elena A Minina
AU - Amélie Bernard
PY - 2026
DA - 2026/05/14
JO - Nature Communications
DO - 10.1038/s41467-026-73116-x
UR - https://hal.science/hal-05773181v1
AB - Autophagy is a conserved intracellular catabolic process, critical for plant stress tolerance. Upon their delivery in the vacuole, how autophagic bodies containing cargo are hydrolyzed to warrant autophagy degradation remains unclear in multicellular organisms. Here, we found that two Arabidopsis phospholipases, LCAT4 and LCAT3, traffic to the vacuolar lumen and converge on autophagic bodies through fundamentally different routes. While LCAT4 directly binds ATG8 and uses autophagy as a transport system to reach the vacuole prepackaged within autophagosomes, LCAT3 traffics to the lytic compartment independently of autophagosome formation. Knocking out both genes causes an accumulation of autophagic bodies accompanied with a reduction in autophagy degradation. In vivo reconstitution demonstrated that LCAT3 can hydrolyse the membrane of autophagic bodies, enabling the activity of LCAT4 to enhance this process. Together, this work sheds light on the vacuolar stages of autophagy, showing that plants have evolved a multi-component pathway for the efficient disruption of autophagosomal membranes as a critical step for the completion of the autophagy pathway.
SN - 2041-1723
SN - 2041-1723
ER -