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Biochemical and biological functions of class I phosphatidylinositol transfer proteins

Cockcroft, S; Carvou, N; (2007) Biochemical and biological functions of class I phosphatidylinositol transfer proteins. BBA-MOL CELL BIOL L , 1771 (6) 677 - 691. 10.1016/j.bbalip.2007.03.009.

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Abstract

Phosphoinositides function in a diverse array of cellular activities. They include a role as substrate for lipid kinases and phospholipases to generate second messengers, regulators of the cytoskeleton, of enzymes and of ion channels, and docking sites for reversible recruitment of proteins to membranes. Mammalian phosphatidylinositol transfer proteins, PITP alpha and PITP beta are paralogs that share 77% sequence identity and contain a hydrophobic cavity that can sequester either phosphatidylinositol or phosphatidylcholine. A string of 11 amino acid residues at the C-terminal acts as a "lid" which shields the lipid from the aqueous environment. PITPs in vitro can facilitate inter-membrane lipid transfer and this requires the movement of the "lid" to allow the lipid cargo to be released. Thus PITPs are structurally designed for delivering lipid cargo and could thus participate in cellular events that are dependent on phosphatidylinositol or derivatives of phosphatidylinositol. Phosphatidylinositol, the precursor for all phosphoinositides is synthesised at the endoplasmic reticulum and its distribution to other organelles could be facilitated by PITPs. Here we highlight recent studies that report on the three-dimensional structures of the different PITP forms and suggest how PITPs are likely to dock at the membrane surface for lipid delivery and extraction. Additionally we discuss whether PITPs are important regulators of sphingomyelin metabolism, and finally describe recent studies that link the association of PITPs with diverse functions including membrane traffic at the Golgi, neurite outgrowth, cytokinesis and stem cell growth. (c) 2007 Elsevier B.V. All rights reserved.

Type: Article
Title: Biochemical and biological functions of class I phosphatidylinositol transfer proteins
DOI: 10.1016/j.bbalip.2007.03.009
Keywords: sphingomyelin, lipid transport, Golgi, netrin-1, cytokinesis, phosphoinositide, phospholipase C, C-DEPENDENT PHOSPHORYLATION, PHOSPHOLIPASE-C, SACCHAROMYCES-CEREVISIAE, CLEAVAGE-FURROW, PLASMA-MEMBRANE, SCHIZOSACCHAROMYCES-POMBE, ENDOPLASMIC-RETICULUM, 4-PHOSPHATE 5-KINASE, SIGNAL-TRANSDUCTION, GENOME SEQUENCE
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Cell and Developmental Biology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Neuro, Physiology and Pharmacology
URI: http://discovery.ucl.ac.uk/id/eprint/189835
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