CALEOSIN 1 interaction with AUTOPHAGY-RELATED PROTEIN 8 facilitates lipid droplet microautophagy in seedlings.
Journal
Plant physiology
ISSN: 1532-2548
Titre abrégé: Plant Physiol
Pays: United States
ID NLM: 0401224
Informations de publication
Date de publication:
22 Nov 2023
22 Nov 2023
Historique:
received:
21
04
2023
accepted:
05
08
2023
medline:
23
11
2023
pubmed:
25
8
2023
entrez:
24
8
2023
Statut:
ppublish
Résumé
Lipid droplets (LDs) of seed tissues are storage organelles for triacylglycerols (TAGs) that provide the energy and carbon for seedling establishment. In the major route of LD degradation (lipolysis), TAGs are mobilized by lipases. However, LDs may also be degraded via lipophagy, a type of selective autophagy, which mediates LD delivery to vacuoles or lysosomes. The exact mechanisms of LD degradation and the mobilization of their content in plants remain unresolved. Here, we provide evidence that LDs are degraded via a process morphologically resembling microlipophagy in Arabidopsis (Arabidopsis thaliana) seedlings. We observed the entry and presence of LDs in the central vacuole as well as their breakdown. Moreover, we show co-localization of AUTOPHAGY-RELATED PROTEIN 8b (ATG8b) and LDs during seed germination and localization of lipidated ATG8 (ATG8-PE) to the LD fraction. We further demonstrate that structural LD proteins from the caleosin family, CALEOSIN 1 (CLO1), CALEOSIN 2 (CLO2), and CALEOSIN 3 (CLO3), interact with ATG8 proteins and possess putative ATG8-interacting motifs (AIMs). Deletion of the AIM localized directly before the proline knot disrupts the interaction of CLO1 with ATG8b, suggesting a possible role of this region in the interaction between these proteins. Collectively, we provide insights into LD degradation by microlipophagy in germinating seeds with a particular focus on the role of structural LD proteins in this process.
Identifiants
pubmed: 37619984
pii: 7250430
doi: 10.1093/plphys/kiad471
pmc: PMC10663143
doi:
Substances chimiques
Autophagy-Related Proteins
0
caleosin protein, Sesamum indicum
0
Triglycerides
0
peroxygenase
EC 1.14.-
ATG8 protein, Arabidopsis
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2361-2380Subventions
Organisme : Polish Ministry of Science and Higher Education
ID : 1643/MOB/V/2017/0
Organisme : Polish National Science Centre
ID : UMO-2019/34/E/NZ1/00023
Informations de copyright
© The Author(s) 2023. Published by Oxford University Press on behalf of American Society of Plant Biologists.
Déclaration de conflit d'intérêts
Conflict of interest statement. None declared.
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