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Regulation of phosphoinositide signaling by the inositol polyphosphate 5‐phosphatases
Author(s) -
Astle Megan V.,
Seaton Gillian,
Davies Elizabeth M.,
Fedele Clare G.,
Rahman Parvin,
Arsala Laima,
Mitchell Christina A.
Publication year - 2006
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540600871159
Subject(s) - inositol , polyphosphate , phosphatase , microbiology and biotechnology , second messenger system , intracellular , inositol phosphate , biology , signal transduction , vesicle , biochemistry , phosphorylation , phosphate , receptor , membrane
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