| First Author | Kanoh H | Year | 1997 |
| Journal | Biochim Biophys Acta | Volume | 1348 |
| Issue | 1-2 | Pages | 56-62 |
| PubMed ID | 9370316 | Mgi Jnum | J:43597 |
| Mgi Id | MGI:1098084 | Doi | 10.1016/s0005-2760(97)00094-5 |
| Citation | Kanoh H, et al. (1997) Phosphatidic acid phosphatase from mammalian tissues: discovery of channel-like proteins with unexpected functions. Biochim Biophys Acta 1348(1-2):56-62 |
| abstractText | 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. |
