Difference between revisions of "Phosphatase Subfamily PTPMT1"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1I|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_PTPMT1|Subfamily PTPMT1]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1I|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_PTPMT1|Subfamily PTPMT1]] | ||
| + | === Evolution === | ||
| + | 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 <cite>Teh13</cite>. | ||
| − | PTPMT1 | + | === Domain === |
| + | PTPMT1 has a single domain: phosphatase domain. It has a mitochondria-targeting sequence on N-terminus. | ||
| − | + | === Function === | |
| + | PTPMT1 (or PLIP) is the first member of PTP superfamily found exclusively localized to the mitochondrion <cite>pmid16039589</cite>. It was originally discovered as an open reading frame encoding a phosphatase with sequence similarity to the tumor suppressor PTEN <cite>pmid15247229</cite>. Like PTEN, PTPMT1 possesses very poor activity toward proteinaceous substrates <cite>pmid15247229</cite>. In vitro, it specifically dephosphorylates phosphatidylinositol 5-phosphate (PI5P), displaying much less activity against any other phosphoinositides <cite>pmid15247229</cite>. However, depletion of PTPMT1 in cells produces no effect on the cellular level of PI5P, suggesting that PI5P is not the endogenous substrate <cite>pmid16039589</cite>. 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 <cite>zhang11</cite>. | ||
| − | == | + | === Acknowledgement === |
| + | Thank Ji Zhang at UC San Diego for her contribution. | ||
| + | == References == | ||
<biblio> | <biblio> | ||
#zhang11 pmid=21641550 | #zhang11 pmid=21641550 | ||
Revision as of 05:11, 27 February 2015
Phosphatase Classification: Superfamily CC1: Family DSP: Subfamily PTPMT1
Evolution
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 [1].
Domain
PTPMT1 has a single domain: phosphatase domain. It has a mitochondria-targeting sequence on N-terminus.
Function
PTPMT1 (or PLIP) is the first member of PTP superfamily found exclusively localized to the mitochondrion [2]. It was originally discovered as an open reading frame encoding a phosphatase with sequence similarity to the tumor suppressor PTEN [3]. Like PTEN, PTPMT1 possesses very poor activity toward proteinaceous substrates [3]. In vitro, it specifically dephosphorylates phosphatidylinositol 5-phosphate (PI5P), displaying much less activity against any other phosphoinositides [3]. However, depletion of PTPMT1 in cells produces no effect on the cellular level of PI5P, suggesting that PI5P is not the endogenous substrate [2]. 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 [4].
Acknowledgement
Thank Ji Zhang at UC San Diego for her contribution.
References
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Error fetching PMID 15247229:
Error fetching PMID 16039589:
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- Error fetching PMID 15247229:
- Error fetching PMID 21641550:
