Abstract：
:PTPMT1 was the first protein tyrosine phosphatase found localized to the mitochondria, but its biological function was unknown. Herein, we demonstrate that whole body deletion of Ptpmt1 in mice leads to embryonic lethality, suggesting an indispensable role for PTPMT1 during development. 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 phosphatidylglycerophosphate (PGP) along with a concomitant decrease in phosphatidylglycerol. PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. We further demonstrate that PTPMT1 specifically dephosphorylates PGP in vitro. Loss of PTPMT1 leads to dramatic diminution of cardiolipin, which can be partially reversed by the expression of catalytic active PTPMT1. Our study identifies PTPMT1 as the mammalian PGP phosphatase and points to its role as a regulator of cardiolipin biosynthesis.
journal_name
Cell Metabjournal_title
Cell metabolismauthors
Zhang J,Guan Z,Murphy AN,Wiley SE,Perkins GA,Worby CA,Engel JL,Heacock P,Nguyen OK,Wang JH,Raetz CR,Dowhan W,Dixon JEdoi
10.1016/j.cmet.2011.04.007subject
Has Abstractpub_date
2011-06-08 00:00:00pages
690-700issue
6eissn
1550-4131issn
1932-7420pii
S1550-4131(11)00174-4journal_volume
13pub_type
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