@article {2401,
	title = {Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface},
	journal = {Plant Cell},
	volume = {21},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 448XRTimes Cited: 13Cited Reference Count: 42DeBono, Allan Yeats, Trevor H. Rose, Jocelyn K. C. Bird, David Jetter, Reinhard Kunst, Ljerka Samuelsa, Lacey},
	month = {Apr},
	pages = {1230-1238},
	type = {Article},
	abstract = {Plant epidermal cells dedicate more than half of their lipid metabolism to the synthesis of cuticular lipids, which seal and protect the plant shoot. The cuticle is made up of a cutin polymer and waxes, diverse hydrophobic compounds including very-long-chain fatty acids and their derivatives. How such hydrophobic compounds are exported to the cuticle, especially through the hydrophilic plant cell wall, is not known. By performing a reverse genetic screen, we have identified LTPG, a glycosylphosphatidylinositol-anchored lipid transfer protein that is highly expressed in the epidermis during cuticle biosynthesis in Arabidopsis thaliana inflorescence stems. Mutant plant lines with decreased LTPG expression had reduced wax load on the stem surface, showing that LTPG is involved either directly or indirectly in cuticular lipid deposition. In vitro 2-p-toluidinonaphthalene-6-sulfonate assays showed that recombinant LTPG has the capacity to bind to this lipid probe. LTPG was primarily localized to the plasma membrane on all faces of stem epidermal cells in the growing regions of inflorescence stems where wax is actively secreted. These data suggest that LTPG may function as a component of the cuticular lipid export machinery.},
	keywords = {ABC TRANSPORTER, BINDING, CELLS, CUTICULAR WAX, GENE, GENOME-WIDE, MEMBRANE-PROTEINS, PHOSPHOLIPASE-D, PREDICTION SERVER, SEQUENCE TAGS},
	isbn = {1040-4651},
	url = {<Go to ISI>://000266295800020},
	author = {DeBono, A. and Yeats, T. H. and Rose, J. K. C. and Bird, D. and Jetter, R. and Kunst, L. and Samuelsa, L.}
}
