PTPMT1 Protein

Protein tyrosine phosphatase, mitochondrial 1

PTPMT1 Products

PTPMT1 Protein, Recombinant

Molecule	Species	Description	Cat. No
PTPMT1	Human	PTPMT1 Protein, Recombinant	12902-H07E

PTPMT1 Related Areas

Enzyme>>Phosphatase & Regulator>>PTPMT1

Signal Transduction>>Phosphatase & Regulator>> PTPMT1

Enzyme>>Lipid Metabolism Enzymes>> PTPMT1

PTPMT1 Alternative Names

PNAS-129, DUSP23, MOSP, PLIP [Homo sapiens]

1110001D10Rik, 2810004N20Rik, PLIP [Mus musculus]

PTPMT1 Background

PTPMT1 (PTP localized to the Mitochondrion 1) is a member of the protein tyrosine phosphatase superfamily that is localized exclusively to the mitochondrion. It has been recently reported that PTPMT1 dephosphorylates phosphatidylglycerol phosphate, an essential intermediate of cardiolipin biosynthesis. PTPMT1 deficiency in mouse embryonic fibroblasts compromises mitochondrial respiration and results in abnormal mitochondrial morphology. Lipid analysis of PTPMT1-deficient fibroblasts reveals an accumulation of PGP along with a concomitant decrease in phosphatidylglycerol. Modulation of mitochondrial ATP synthesis by PTPMT1 suggests a novel approach for the treatment of pancreatic cancers, which represent some of the deadliest forms of human tumors. The gluttony of cancer cells for energy is well established, and with the development of a modulator of expression, one may hope that we could also achieve the synthetic induction of PTPMT1 expression. It would then be expected that this effect would attenuate, if not abolish, the growth of pancreas-derived tumor cells and support the establishment of a novel regimen for pancreatic cancers. 

PTPMT1 Related Studies

1. Zhang J, et al. (2011) Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis. Cell Metab. 13 (6): 690-700.
2. Boisclair Y, et al. (2005) Firing up mitochondrial activities with PTPMT1. Mol Cell. 19 (3): 291-2.
3. Xiao J, et al. (2011) Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis. Proc Natl Acad Sci. 108 (29): 11860-5.