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How does SHIP 1/2 balance Ptd I ns(3,4) P 2 and does it signal independently of its phosphatase activity?
Author(s) -
Xie Jingwei,
Erneux Christophe,
Pirson Isabelle
Publication year - 2013
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201200168
Subject(s) - cytoskeleton , microbiology and biotechnology , phosphatase , signal transduction , endocytosis , second messenger system , insulin receptor , cell signaling , inositol , biology , scaffold protein , phosphorylation , chemistry , receptor , cell , insulin , biochemistry , insulin resistance , endocrinology
The number of cellular events identified as being directly or indirectly modulated by phosphoinositides dramatically increased in the recent years. Part of the complexity results from the fact that the seven phosphoinositides play second messenger functions in many different areas of growth factors and insulin signaling, cytoskeletal organization, membrane dynamics, trafficking, or nuclear signaling. PtdIns(3,4)P 2 is commonly reported as a product of the SH2 domain‐containing inositol 5‐phosphatases 1/2 (SHIP1 and SHIP2) that dephosphorylate PtdIns(3,4,5)P 3 at the 5‐position. Here we discuss recent interest in PtdIns(3,4)P 2 signaling highlighting its involvement in key cellular mechanisms such as cell adhesion, migration, and cytoskeletal regulation. We question and discuss the involvement of SHIP2 either as a PI 5‐phosphatase or as a scaffold protein in insulin signaling, cytoskeletal dynamics, and endocytosis of growth factor receptors.