Kien_2018_J.Lipid.Res_59_2360

Reference

Title : ABHD5 stimulates PNPLA1-mediated omega-O-acylceramide biosynthesis essential for a functional skin permeability barrier - Kien_2018_J.Lipid.Res_59_2360
Author(s) : Kien B , Grond S , Haemmerle G , Lass A , Eichmann TO , Radner FPW
Ref : J Lipid Res , 59 :2360 , 2018
Abstract :

Mutations in the genes coding for patatin-like phospholipase domain-containing 1 (PNPLA1) and alpha/beta-hydrolase domain-containing 5 (ABHD5), also known as comparative gene identification 58, are causative for ichthyosis, a severe skin barrier disorder. Individuals with mutations in either of these genes show a defect in epidermal omega-O-acylceramide (AcylCer) biosynthesis, suggesting that PNPLA1 and ABHD5 act in the same metabolic pathway. In this report, we identified ABHD5 as a coactivator of PNPLA1 that stimulates the esterification of omega-hydroxy ceramides with linoleic acid for AcylCer biosynthesis. ABHD5 interacts with PNPLA1 and recruits the enzyme to its putative triacylglycerol substrate onto cytosolic lipid droplets. Conversely, alleles of ABHD5 carrying point mutations associated with ichthyosis in humans failed to accelerate PNPLA1-mediated AcylCer biosynthesis. Our findings establish an important biochemical function of ABHD5 in interacting with PNPLA1 to synthesize crucial epidermal lipids, emphasizing the significance of these proteins in the formation of a functional skin permeability barrier.

PubMedSearch : Kien_2018_J.Lipid.Res_59_2360
PubMedID: 30361410
Gene_locus related to this paper: human-ABHD5

Related information

Gene_locus human-ABHD5
Family human-ABHD5    CGI-58_ABHD5_ABHD4

Citations formats

Kien B, Grond S, Haemmerle G, Lass A, Eichmann TO, Radner FPW (2018)
ABHD5 stimulates PNPLA1-mediated omega-O-acylceramide biosynthesis essential for a functional skin permeability barrier
J Lipid Res 59 :2360

Kien B, Grond S, Haemmerle G, Lass A, Eichmann TO, Radner FPW (2018)
J Lipid Res 59 :2360