High impact information on TPTE2

• TPIP has a wider tissue distribution than the testis-specific TPTE, with specific splice variants being expressed in testis, brain and stomach [1].
• TPIP alpha displays similar phosphoinositide 3-phosphatase activity compared with PTEN against PtdIns(3,4,5)P(3), PtdIns(3,5)P(2), PtdIns(3,4)P(2) and PtdIns(3)P, has N-terminal transmembrane domains and appears to be localized on the endoplasmic reticulum [1].
• TPTE and TPIP do not appear to be functional orthologues of the Golgi-localized and more distantly related murine PTEN2 [1].
• TPIP: a novel phosphoinositide 3-phosphatase [1].
• The results underline the effective shielding of the lanthanide by the twelve phenyl groups of the tpip ligands and the reduction of high-energy vibrations in close proximity to the lanthanide, both features important in the design of NIR emitting lanthanide complexes [2].

Anatomical context of TPTE2

• We suggest that TPIP alpha plays a role in regulating phosphoinositide signalling on the endoplasmic reticulum, and might also represent a tumour suppressor and functional homologue of PTEN in some tissues [1].
• In the present study, we show that TPTE and TPIP proteins are expressed in secondary spermatocytes and/or prespermatids [3].

References