Arabidopsis CaLB1 undergoes phase separation with the ESCRT protein ALIX and modulates autophagosome maturation.
Arabidopsis
/ metabolism
Autophagosomes
/ metabolism
Endosomal Sorting Complexes Required for Transport
/ metabolism
Arabidopsis Proteins
/ metabolism
Calcium-Binding Proteins
/ metabolism
Autophagy
Phosphatidylinositol Phosphates
/ metabolism
Autophagy-Related Protein 8 Family
/ metabolism
Vacuoles
/ metabolism
Phase Separation
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
19 Jun 2024
19 Jun 2024
Historique:
received:
15
08
2023
accepted:
05
06
2024
medline:
20
6
2024
pubmed:
20
6
2024
entrez:
19
6
2024
Statut:
epublish
Résumé
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 Ca
Identifiants
pubmed: 38898014
doi: 10.1038/s41467-024-49485-6
pii: 10.1038/s41467-024-49485-6
doi:
Substances chimiques
Endosomal Sorting Complexes Required for Transport
0
Arabidopsis Proteins
0
Calcium-Binding Proteins
0
Phosphatidylinositol Phosphates
0
phosphatidylinositol 3-phosphate
0
Autophagy-Related Protein 8 Family
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
5188Subventions
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 189682160
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : SFB969
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : INST 38/579-1
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : SFB969
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 496470458
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : SFB 969
Informations de copyright
© 2024. The Author(s).
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