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

Matthew J Wishart; Jack E Dixon

doi:10.1016/s0962-8924(02)02412-1

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

Trends Cell Biol. 2002 Dec;12(12):579-85. doi: 10.1016/s0962-8924(02)02412-1.

Authors

Matthew J Wishart¹, Jack E Dixon

Affiliation

¹ Dept of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, USA.

PMID: 12495846
DOI: 10.1016/s0962-8924(02)02412-1

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

MeSH terms

Disease*
Humans
PTEN Phosphohydrolase
Phosphatidylinositols / metabolism*
Phosphoric Monoester Hydrolases / chemistry
Phosphoric Monoester Hydrolases / metabolism*
Phosphorylation
Protein Tyrosine Phosphatases / chemistry
Protein Tyrosine Phosphatases / metabolism*
Protein Tyrosine Phosphatases, Non-Receptor
Tumor Suppressor Proteins / chemistry
Tumor Suppressor Proteins / metabolism*

Substances

Phosphatidylinositols
Tumor Suppressor Proteins
Phosphoric Monoester Hydrolases
Protein Tyrosine Phosphatases
Protein Tyrosine Phosphatases, Non-Receptor
myotubularin
PTEN Phosphohydrolase
PTEN protein, human