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An involvement of phospholipase A/acyltransferase family proteins in peroxisome regulation and plasmalogen metabolism
Author(s) -
Uyama Toru,
Tsuboi Kazuhito,
Ueda Natsuo
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12787
Subject(s) - plasmalogen , acyltransferase , peroxisome , biogenesis , biochemistry , acyltransferases , enzyme , biology , phospholipid , phospholipase , metabolism , lipid metabolism , chemistry , biosynthesis , receptor , gene , membrane
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 HRASLS 1–5 as PLA/acyltransferase ( PLAAT )‐1–5. Notably, PLAAT s 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 PEX 19. In this article, we will review our recent findings about PLAAT proteins, with special reference to their roles in peroxisome biogenesis and plasmalogen metabolism.