Abstract
Phosphoinositide 3-kinases (PI3Ks) phosphorylate the 3′-OH position of the inositol ring of inositol phospholipids, producing three lipid products: PtdIns(3)P, PtdIns(3,4)P2 and PtdIns(3,4,5)P3. These lipids bind to the pleckstrin homology (PH) domains of proteins and control the activity and subcellular localisation of a diverse array of signal transduction molecules. Three major classes of signalling molecule are regulated by binding of D-3 phosphoinositides to PH domains: guanine-nucleotide-exchange proteins for Rho family GTPases, the TEC family tyrosine kinases such as BTK and ITK in B and T lymphocytes, respectively, and the AGC superfamily of serine/threonine protein kinases. These molecules are activated by a variety of extracellular stimuli and have been implicated in a wide range of cellular processes, including cell cycle progression, cell growth, cell motility, cell adhesion and cell survival.
Original language | English |
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Pages (from-to) | 1439-1445 |
Number of pages | 7 |
Journal | Journal of Cell Science |
Volume | 114 |
Issue number | 8 |
Publication status | Published - 15 Apr 2001 |
Keywords
- PH domains
- Phosphoinositide 3-kinase
- Protein kinase B
- Rac-1
- Tec kinases
ASJC Scopus subject areas
- Cell Biology