Difference between revisions of "Phosphatase Subfamily PTPMT1"
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| − | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1I|Superfamily CC1]]: [[ | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1I|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_PTPMT1|Subfamily PTPMT1]] |
Revision as of 01:27, 28 December 2014
Phosphatase Classification: Superfamily CC1: Family DSP: Subfamily PTPMT1
PTPMT1 (or PLIP) is the first member of PTP superfamily found exclusively localized to the mitochondrion [1]. It was originally discovered as an open reading frame encoding a phosphatase with sequence similarity to the tumor suppressor PTEN [2]. Like PTEN, PTPMT1 possesses very poor activity toward proteinaceous substrates [2]. In vitro, it specifically dephosphorylates phosphatidylinositol 5-phosphate (PI5P), displaying much less activity against any other phosphoinositides [2]. However, depletion of PTPMT1 in cells produces no effect on the cellular level of PI5P, suggesting that PI5P is not the endogenous substrate [1]. Later, it has been found that PTPMT1 is a mitochondrial phosphatase that converts phosphatidylglycerolphosphate (PGP) to phosphatidylglycerol, a critical step in the de novo biosynthesis of cardiolipin [3]. It is found in most or all animals and higher plants, but is absent from fungi, Monosiga, and lower plants. It is also found in several protists, including Dictyostelium , Leishamania, Trypanosomes, Ectocarpus, and diatoms. More surprisingly, a functional PTPMT1 is found in a eubacterium Rhodopirellula baltica [4].
Acknowledgement. Thank Ji Zhang at UC San Diego for her contribution.
References
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