Modular phosphoinositide-binding domains - their role in signalling and membrane trafficking

Citation
Pj. Cullen et al., Modular phosphoinositide-binding domains - their role in signalling and membrane trafficking, CURR BIOL, 11(21), 2001, pp. R882-R893
Citations number
102
Categorie Soggetti
Experimental Biology
Journal title
CURRENT BIOLOGY
ISSN journal
09609822 → ACNP
Volume
11
Issue
21
Year of publication
2001
Pages
R882 - R893
Database
ISI
SICI code
0960-9822(20011030)11:21<R882:MPD-TR>2.0.ZU;2-7
Abstract
The membrane phospholipid phosphatidylinositol is the precursor of a family of lipid second-messengers, known as phosphoinositides, which differ in th e phosphorylation status of their inositol group. A major advance in unders tanding phosphoinositide signalling has been the identification of a number of highly conserved modular protein domains whose function appears to be t o bind various phosphoinositides. Such 'cut and pastel modules are found in a diverse array of multidomain proteins and recruit their host protein to specific regions in cells via interactions with phosphoinositides. Here, wi th particular reference to proteins involved in membrane traffic pathways, we discuss recent advances in our understanding of phosphoinasitide-binding domains.