CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo.
Drosophila
LDAF1
Ldo16
Ldo45
Lipid droplets
Lipid metabolism
Promethin
Seipin
TMEM159
lipid droplet biogenesis
lipid storage
Journal
Insect biochemistry and molecular biology
ISSN: 1879-0240
Titre abrégé: Insect Biochem Mol Biol
Pays: England
ID NLM: 9207282
Informations de publication
Date de publication:
06 2021
06 2021
Historique:
received:
15
07
2020
revised:
05
11
2020
accepted:
29
11
2020
pubmed:
12
12
2020
medline:
8
9
2021
entrez:
11
12
2020
Statut:
ppublish
Résumé
The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The function of LDAF1 proteins outside mammals is less clear. In yeast, the lipid droplet organization (LDO) proteins, which also cooperate with Seipin, are the putative homologs of LDAF1. While certain functional aspects are shared between the LDO and mammalian LDAF1 proteins, the relationship between the proteins is under debate. Here, we identify the Drosophila melanogaster protein CG32803, which we re-named to dmLDAF1, as an insect member of this protein family. dmLDAF1 decorates LDs in cultured cells and in vivo and the protein is linked to the fly and mouse Seipin proteins. Altering the dmLDAF1 abundance affects LD size, number and overall lipid storage amounts. Our results suggest that the LDAF1 proteins thus fulfill an evolutionarily conserved function in the biogenesis and biology of LDs.
Identifiants
pubmed: 33307187
pii: S0965-1748(20)30201-0
doi: 10.1016/j.ibmb.2020.103512
pii:
doi:
Substances chimiques
BSCL2 protein, human
0
Drosophila Proteins
0
GTP-Binding Protein gamma Subunits
0
Membrane Proteins
0
TMEM159 protein, human
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
103512Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.