Absence of ATG9A and synaptophysin demixing on Rab5 mutation-induced giant endosomes.
Mol Brain
; 17(1): 63, 2024 Sep 02.
Article
in En
| MEDLINE
| ID: mdl-39223639
ABSTRACT
ATG9A is the only integral membrane protein among core autophagy-related (ATG) proteins. We previously found that ATG9A does not co-assemble into synaptophysin-positive vesicles, but rather, localizes to a distinct pool of vesicles within synapsin condensates in both fibroblasts and nerve terminals. The endocytic origin of these vesicles further suggests the existence of different intracellular sorting or segregation mechanisms for ATG9A and synaptophysin in cells. However, the precise underlying mechanism remains largely unknown. In this follow-up study, we investigated the endosomal localization of these two proteins by exploiting the advantages of a Rab5 mutant that induces the formation of enlarged endosomes. Notably, ATG9A and synaptophysin intermix perfectly and do not segregate on giant endosomes, indicating that the separation of these two proteins is not solely caused by the inherent properties of the proteins, but possibly by other unknown factors.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endosomes
/
Synaptophysin
/
Rab5 GTP-Binding Proteins
/
Autophagy-Related Proteins
/
Mutation
Limits:
Animals
/
Humans
Language:
En
Journal:
Mol Brain
Journal subject:
BIOLOGIA MOLECULAR
/
CEREBRO
Year:
2024
Document type:
Article
Affiliation country:
Corea del Sur