The Golgi-localized sphingosine-1-phosphate phosphatase is indispensable for Leishmania major.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
26 09 2022
26 09 2022
Historique:
received:
04
06
2022
accepted:
12
09
2022
entrez:
27
9
2022
pubmed:
28
9
2022
medline:
1
10
2022
Statut:
epublish
Résumé
Sphingosine-1-phosphate phosphatase (SPP) catalyzes the dephosphorylation of sphingosine-1-phosphate (S1P) into sphingosine, the reverse reaction of sphingosine kinase. In mammals, S1P acts as a potent bioactive molecule regulating cell proliferation, migration, and immunity. In Leishmania, S1P production is crucial for the synthesis of ethanolamine and choline phospholipids, and cell survival under stress conditions. To better understand the roles of S1P, we characterized a SPP ortholog in Leishmania major which displays activity towards S1P but not structurally related lipids such as ceramide-1-phosphate or lysophosphatidic acid. While this enzyme is found in the endoplasmic reticulum in mammalian cells, L. major SPP is localized at the Golgi apparatus. Importantly, chromosomal SPP alleles cannot be deleted from L. major even with the addition of a complementing episome, suggesting that endogenously expressed SPP is essential. Finally, SPP overexpression in L. major leads to a slower growth rate and heightened sensitivity to brefeldin A and sodium orthovanadate. Together, these results suggest that the equilibrium between S1P and sphingosine is vital for the function of Golgi apparatus in Leishmania.
Identifiants
pubmed: 36163400
doi: 10.1038/s41598-022-20249-w
pii: 10.1038/s41598-022-20249-w
pmc: PMC9513092
doi:
Substances chimiques
Ceramides
0
Ethanolamines
0
Lysophospholipids
0
Membrane Proteins
0
Phosphates
0
Brefeldin A
20350-15-6
sphingosine 1-phosphate
26993-30-6
Vanadates
3WHH0066W5
Sodium
9NEZ333N27
sphingosine-1-phosphate phosphatase
EC 3.1.3.-
Phosphoric Monoester Hydrolases
EC 3.1.3.2
Choline
N91BDP6H0X
Sphingosine
NGZ37HRE42
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
16064Subventions
Organisme : NIAID NIH HHS
ID : R01 AI099380
Pays : United States
Organisme : NIAID NIH HHS
ID : R15 AI076909
Pays : United States
Organisme : NIH HHS
ID : AI099380
Pays : United States
Informations de copyright
© 2022. The Author(s).
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