Phosphoinositide signalling in the nucleus

Keune, Willem Jan, Bultsma, Yvette, Sommer, Lilly, Jones, David and Divecha, Nullin (2011) Phosphoinositide signalling in the nucleus. Advances in Enzyme Regulation, 51 (1), 91-99. (doi:10.1016/j.advenzreg.2010.09.009).

Abstract

Phosphorylation at the 3,4, or 5, position of the inositol head group of phosphatidylinositol generates seven different phosphoinositides that form the basis of a ubiquitous membrane signalling system. An array of tightly regulated phosphoinositide kinases and phosphatases, ultimately control the subcellular profile of phosphoinositides (Irvine, 2005). Phosphoinositides can regulate protein localisation, ion channel function and protein enzymatic activity, which can impact on cellular processes including vesicle transport, cytoskeletal dynamics, cell proliferation and survival, gene transcription, cell polarity and migration (McCrea and DeCamilli, 2009). Phosphoinositides are tethered tightly into the membrane and can recruit and localise proteins to specific subcellular membrane domains through specific phosphoinositide interacting domains (PID) (Lemmon, 2003). Because the membrane can be considered more akin to a two dimensional system, membrane interaction is analogous to inducing protein/protein interactions and acts to concentrate upstream regulators and downstream targets together leading to enhanced downstream signalling and specificity. Phosphoinositide signalling occurs on many different intracellular membranes including the inner surface of the plasma membrane, the golgi, the endoplasmic reticulum and on membrane vesicles that move between these compartments and their deregulation had been implicated in an array of human diseases (McCrea and DeCamilli, 2009).

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Contributors

Author: David Jones

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