期刊
MOLECULAR CELL
卷 19, 期 2, 页码 197-207出版社
CELL PRESS
DOI: 10.1016/j.molcel.2005.06.008
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资金
- NIDDK NIH HHS [F32 DK067799] Funding Source: Medline
- NIGMS NIH HHS [2 T32 GM07752-25] Funding Source: Medline
- PHS HHS [18024] Funding Source: Medline
Reversible phosphorylation is the cell's most prevalent form of posttranslational modification, yet its role in the regulation of mitochondrial functions is poorly understood. We have discovered that a member of the dual-specific protein tyrosine phosphatase (DS-PTP) family, PTPMT1 (PTP localized to the Mitochondrion 1) resides nearly exclusively in mitochondria. PTPMT1 is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. Knockdown of PTPMT1 expression in the pancreatic insulinoma cell line INS-1 832/ 13 alters the mitochondrial phosphoprotein profile and markedly enhances both ATP production and insulin secretion. These data define PTPMT1 as a potential drug target for the treatment of type II diabetes and strengthen the notion that mitochondria are an underappreciated site of signaling by reversible phosphorylation.
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