Prospects & Overviews
How does SHIP1/2 balance PtdIns(3,4)P2 and does it signal independently of its phosphatase activity?
Article first published online: 7 MAY 2013
© 2013 WILEY Periodicals, Inc.
Volume 35, Issue 8, pages 733–743, August 2013
How to Cite
Xie, J., Erneux, C. and Pirson, I. (2013), How does SHIP1/2 balance PtdIns(3,4)P2 and does it signal independently of its phosphatase activity?. Bioessays, 35: 733–743. doi: 10.1002/bies.201200168
- Issue published online: 15 JUL 2013
- Article first published online: 7 MAY 2013
- Fonds de la Recherche Scientifique Médicale
- Interuniversity Attraction Poles Programme (P6/28) – Belgium State and Télévie (Belgium)
- EGFR endocytosis;
- scaffold properties;
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)P2 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)P3 at the 5-position. Here we discuss recent interest in PtdIns(3,4)P2 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.