TPIP: a novel phosphoinositide 3-phosphatase
作者： Steven M. WALKER , C. Peter DOWNES , Nick R. LESLIE
DOI: 10.1042/0264-6021:3600277
关键词: Tensin 、 C2 domain 、 Transmembrane protein 、 Transmembrane domain 、 Biochemistry 、 PTEN 、 Phosphoinositide Phosphatases 、 Phosphatase 、 Endoplasmic reticulum 、 Biology
摘要: The PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor is a phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] 3-phosphatase that plays critical role in regulating many cellular processes by antagonizing the phosphoinositide 3-kinase signalling pathway. We have identified characterized two human homologues of PTEN, which differ with respect to their subcellular localization lipid phosphatase activities. previously cloned, but uncharacterized, TPTE (transmembrane homology) localized plasma membrane, lacks detectable activity. TPIP (TPTE homologous inositol phosphatase) novel occurs several differentially spliced forms two, alpha beta, appear be functionally distinct. displays similar activity compared against PtdIns(3,4,5)P(3), PtdIns(3,5)P(2), PtdIns(3,4)P(2) PtdIns(3)P, has N-terminal transmembrane domains appears endoplasmic reticulum. This unusual as most signalling-lipid-metabolizing enzymes are not integral membrane proteins. however, cytosolic. wider tissue distribution than testis-specific TPTE, specific splice variants being expressed testis, brain stomach. do functional orthologues Golgi-localized more distantly related murine PTEN2. suggest reticulum, might also represent some tissues.
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