Journal
FEBS LETTERS
Volume 591, Issue 18, Pages 2745-2760Publisher
WILEY
DOI: 10.1002/1873-3468.12787
Keywords
N-acylethanolamine; N-acyl-plasmalogen; peroxisome
Funding
- Japan Society for the Promotion of Science [15K08278, 17K01852, 16K08589]
- Grants-in-Aid for Scientific Research [15K08278, 16K08589, 17K01852] Funding Source: KAKEN
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The H-Ras-like suppressor (HRASLS) is a protein family consisting of five members in humans. Despite their discovery as tumor suppressors, we demonstrated that all these proteins are phospholipid-metabolizing enzymes, such as phospholipase (PL) A(1)/A(2) and acyltransferase. We thus proposed to rename HRASLS1-5 as PLA/acyltransferase (PLAAT)-1-5. Notably, PLAATs exhibit N-acyltransferase activity to biosynthesize N-acylated ethanolamine phospholipids, including N-acyl-plasmalogen, which serve as precursors of bioactive N-acylethanolamines. Furthermore, the overexpression of PLAAT-3 in animal cells causes disappearance of peroxisomes and a remarkable reduction in plasmalogen levels. This finding might be related to the inhibitory effect of PLAAT-3 on the chaperone activity of the peroxin PEX19. In this article, we will review our recent findings about PLAAT proteins, with special reference to their roles in peroxisome biogenesis and plasmalogen metabolism.
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