PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease

The phosphatase and tensin homolog deleted on chromosome ten (PTEN) and myotubularin (MTM1) represent subfamilies of protein tyrosine phosphatases whose principal physiological substrates are D3-phosphorylated inositol phospholipids. As lipid phosphatases, PTEN- and MTM1-related (MTMR) proteins deph...

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Bibliographic Details
Published in:Trends in cell biology 2002-12, Vol.12 (12), p.579
Main Authors: Wishart, Matthew J, Dixon, Jack E
Format: Article
Language:English
Subjects:
Disease
Humans
Phosphatidylinositols - metabolism
Phosphoric Monoester Hydrolases - chemistry
Phosphoric Monoester Hydrolases - metabolism
Phosphorylation
Protein Tyrosine Phosphatases - chemistry
Protein Tyrosine Phosphatases - metabolism
Protein Tyrosine Phosphatases, Non-Receptor
PTEN Phosphohydrolase
Tumor Suppressor Proteins - chemistry
Tumor Suppressor Proteins - metabolism
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Summary:The phosphatase and tensin homolog deleted on chromosome ten (PTEN) and myotubularin (MTM1) represent subfamilies of protein tyrosine phosphatases whose principal physiological substrates are D3-phosphorylated inositol phospholipids. As lipid phosphatases, PTEN- and MTM1-related (MTMR) proteins dephosphorylate the products of phosphoinositide 3-kinases and antagonize downstream effectors that utilize 3-phosphoinositides as ligands for protein targeting domains or allosteric activation. Here, we describe the cellular mechanisms of PTEN and MTMR function and their role in the etiology of cancer and other human diseases.
ISSN:0962-8924
1879-3088
DOI:10.1016/S0962-8924(02)02412-1