Detection and quantification of the vacuolar H+ATPase using the Legionella effector protein SidK.
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
07 03 2022
07 03 2022
Historique:
received:
29
07
2021
revised:
14
12
2021
accepted:
21
12
2021
entrez:
13
1
2022
pubmed:
14
1
2022
medline:
17
2
2022
Statut:
ppublish
Résumé
Acidification of secretory and endocytic organelles is required for proper receptor recycling, membrane traffic, protein degradation, and solute transport. Proton-pumping vacuolar H+ ATPases (V-ATPases) are responsible for this luminal acidification, which increases progressively as secretory and endocytic vesicles mature. An increasing density of V-ATPase complexes is thought to account for the gradual decrease in pH, but available reagents have not been sufficiently sensitive or specific to test this hypothesis. We introduce a new probe to localize and quantify V-ATPases. The probe is derived from SidK, a Legionella pneumophila effector protein that binds to the V-ATPase A subunit. We generated plasmids encoding fluorescent chimeras of SidK1-278, and labeled recombinant SidK1-278 with Alexa Fluor 568 to visualize and quantify V-ATPases with high specificity in live and fixed cells, respectively. We show that V-ATPases are acquired progressively during phagosome maturation, that they distribute in discrete membrane subdomains, and that their density in lysosomes depends on their subcellular localization.
Identifiants
pubmed: 35024770
pii: 212963
doi: 10.1083/jcb.202107174
pmc: PMC8763849
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Vacuolar Proton-Translocating ATPases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : CIHR
ID : PJT166152
Pays : Canada
Organisme : CIHR
ID : FDN-143202
Pays : Canada
Informations de copyright
© 2022 Maxson et al.
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