Source
Laboratory of Cellular and Molecular Biology, National Institute on Aging/NIH, GRC Bldg., MSC-12, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA.
Abstract
Phosphoinositide 3-kinases (PI3Ks) phosphorylate the D3 position of the myo -inositol ring of inositol phospholipids, producing, amongst others, phosphatidylinositol-(3,4,5)-trisphosphate. This activity is opposed by the lipid phosphatase PTEN, which catalyzes the removal of this phosphate. Stimulation of PI3Ks is elicited by engagement of receptors for antigen, cytokines and chemokines, and by co-stimulatory molecules. Kinases and other enzymes containing pleckstrin homology domains are activated by binding to these phospholipids, affecting a variety of cellular processes that control lymphocyte function, including cell survival, proliferation, chemotaxis and cytoskeletal reorganization. This review highlights the signaling pathways of these kinases and other enzymes in T cells, their biological effects, and their regulation by PTEN.
Copyright 2002 Academic Press.