Regulation of phosphoinositide signaling by the inositol polyphosphate 5‐phosphatases

• Published in: IUBMB life 2006-08, Vol.58 (8), p.451-456
• Main Authors: Astle, Megan V., Seaton, Gillian, Davies, Elizabeth M., Fedele, Clare G., Rahman, Parvin, Arsala, Laima, Mitchell, Christina A.
• Format: Article
• Language: English
• Subjects: 5‐phosphatases; Animals; Humans; Inositol Polyphosphate 5-Phosphatases; Isoenzymes - chemistry; Isoenzymes - genetics; Isoenzymes - metabolism; Models, Biological; Oculocerebrorenal Syndrome - enzymology; Oculocerebrorenal Syndrome - genetics; Phosphatidylinositol 3-Kinases - metabolism; Phosphatidylinositols - metabolism; phosphoinositides; Phosphoric Monoester Hydrolases - chemistry; Phosphoric Monoester Hydrolases - genetics; Phosphoric Monoester Hydrolases - metabolism; PI3‐kinase; Protein Structure, Tertiary; Signal Transduction; Signaling
• ISSN: 1521-6543; 1521-6551
• DOI: 10.1080/15216540600871159

Phosphoinositide signaling molecules control cellular growth, proliferation and differentiation, intracellular vesicle trafficking, and cytoskeletal rearrangement. The inositol polyphosphate 5‐phosphatase family remove the D‐5 position phosphate from PtdIns(3,4,5)P3, PtdIns(4,5)P2 and PtdIns(3,5)P2 forming PtdIns(3,4)P2, PtdIns(4)P and PtdIns(3)P respectively. This enzyme family, comprising ten mammalian members, exhibit seemingly non‐redundant functions including the regulation of synaptic vesicle recycling, hematopoietic cell function and insulin signaling. Here we highlight recently established insights into the functions of two well characterized 5‐phosphatases OCRL and SHIP2, which have been the subject of extensive functional studies, and the characterization of recently identified members, SKIP and PIPP, in order to highlight the diverse and complex functions of this enzyme family. iubmb Life, 58: 451 ‐ 456, 2006