Phospholipase A and acyltransferase 4 (PLAAT4)

Phospholipase A and acyltransferase 4 (PLAAT4) is a membrane-associated enzyme with both phospholipase A1/2 and acyltransferase activities, capable of catalyzing the release and transfer of fatty acids from glycerophospholipids and forming precursors of bioactive lipids such as N-acylphosphatidylethanolamines[1][2][6][8]. PLAAT4 is induced by retinoids (notably tazarotene) via retinoic acid receptor signaling and acts as a tumor suppressor, promoting growth inhibition, cell differentiation, and apoptosis, particularly in epithelial tissues. Structurally, PLAAT4 contains a conserved catalytic triad essential for its enzymatic function and a transmembrane domain that targets it to cell membranes (plasma membrane, ER, Golgi)[2][6]. PLAAT4 has shown roles in keratinocyte differentiation (through association with transglutaminase 1), restriction of intracellular pathogens (including Toxoplasma gondii), and as a regulator in cancer and hyperproliferative disorders. Its gene is upregulated in response to retinoid therapies and may serve as a biomarker for retinoid responsiveness and tumor suppression[1][2][8].

Other names

TIG3RIG1HRASLS4PLAAT-4RARRES3Retinoic acid receptor responder (tazarotene induced) 3Retinoic acid receptor responder protein 3Retinoid-inducible gene 1 proteinTazarotene-induced gene 3 proteinHRSL4PLA1/2-3

Drugs (retinoids) upregulate PLAAT4 expression via nuclear retinoic acid receptors, inducing anti-proliferative and pro-differentiation effects