Phosphoinositide phosphatases in a network of signalling reactions.

Abstract

Phosphoinositide phosphatases dephosphorylate the three positions (D-3, 4 and 5) of the inositol ring of the poly-phosphoinositides. They belong to different families of enzymes. The PtdIns(3,4)P(2) 4-phosphatase family, the tumour suppressor phosphatase and tensin homolog deleted on chromosome 10 (PTEN), SAC1 domain phosphatases and myotubularins belong to the tyrosine protein phosphatases superfamily. They share the presence of a conserved cysteine residue in the consensus CX(5)RT/S. Another family consists of the inositol polyphosphate 5-phosphatase isoenzymes. The importance of these phosphoinositide phosphatases in cell regulation is illustrated by multiple examples of their implications in human diseases such as Lowe syndrome, X-linked myotubular myopathy, cancer, diabetes or bacterial infection.

• Authors: Daniel Blero, Bernard Payrastre, Stéphane Schurmans, Christophe Erneux
• Journal: Pflugers Archiv : European journal of physiology (Pflugers Arch) Vol. 455 Issue 1 Pg. 31-44 (Oct 2007) ISSN: 0031-6768 [Print] Germany
• PMID: 17605038 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Isoenzymes
• Phosphatidylinositols
• Inositol 1,4,5-Trisphosphate
• Phosphoric Monoester Hydrolases
• PTEN Phosphohydrolase

Topics

• Animals
• Humans
• Inositol 1,4,5-Trisphosphate (genetics, metabolism)
• Isoenzymes (genetics, metabolism)
• PTEN Phosphohydrolase (genetics, metabolism)
• Phosphatidylinositols (metabolism)
• Phosphoric Monoester Hydrolases (genetics, physiology)
• Signal Transduction (genetics, physiology)