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Biochim Biophys Acta. 1997 Sep 4;1348(1-2):56-62.

Phosphatidic acid phosphatase from mammalian tissues: discovery of channel-like proteins with unexpected functions.

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Department of Biochemistry, Sapporo Medical University, School of Medicine, Japan.


Phosphatidic acid phosphatase (PAP) has long been known as a key enzyme involved in both glycerolipid biosynthesis and cellular signal transduction. The cDNA cloning of a plasma membrane-bound type 2 PAP has revealed the existence of a novel glycoprotein with six transmembrane domains. The type 2 PAP now represents an enzyme family consisting of Drosophila Wunen and rat Dri 42, which participate in germ cell migration and epithelial differentiation, respectively. Such novel functions of the type 2 PAP suggest the unexpected importance of lipids and/or their metabolic enzymes.

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