Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 21 March 2000
Vol. 2000, Issue 24, p. tw8
[DOI: 10.1126/stke.2000.24.tw8]

EDITORS' CHOICE

Review A Boatload of SHIP

Signal transduction requires a delicate balance between proteins that have positive regulatory roles and those that have negative ones. It is increasingly evident that negative regulators are just as important as the signal-activating proteins that sometimes garner more attention. The Src homology 2-containing inositol phosphatase (SHIP) protein, an important negative regulator of cell proliferation, contains several protein domains that bind to separate proteins. SHIP functions to remove the 5' phosphate from phosphatidylinositol (PI) 3,4,5-trisphosphate (PIP3), and from PI 1,3,4,5-tetrakisphosphate (PIP4). However, SHIP activity requires the presence of phosphate at the 3' position of PIP3 or PIP4. Rohrschneider et al. review the family of SHIP isoforms and their roles in specific signaling pathways. The authors discuss the importance of protein-protein associations and of recruitment to the plasma membrane for SHIP functionality. SHIP proteins have been found in many different cells; however, Rohrschneider et al. discuss the role of SHIP in negative signaling in the best understood systems--B cells and myeloid cells.

Rohrschneider, L.R., Fuller, J.F., Wolf, I., Liu, Y., and Lucas, D.M. (2000) Structure, function, and biology of SHIP proteins. Genes Dev. 14: 505-520. [Full Text]

Citation: A Boatload of SHIP. Sci. STKE 2000, tw8 (2000).



To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882