Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface

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 su...

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Published inThe Plant cell Vol. 21; no. 4; pp. 1230 - 1238
Main Authors DeBono, Allan, Yeats, Trevor H, Rose, Jocelyn K.C, Bird, David, Jetter, Reinhard, Kunst, Ljerka, Samuels, Lacey
Format Journal Article
LanguageEnglish
Published United States American Society of Plant Biologists 01.04.2009
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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.
AbstractList 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.
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.
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.
Author Kunst, Ljerka
Samuels, Lacey
Rose, Jocelyn K.C
Bird, David
Jetter, Reinhard
DeBono, Allan
Yeats, Trevor H
AuthorAffiliation a Department of Botany, University of British Columbia, Vancouver, BC, Canada V6T 1Z4
c Department of Chemistry, University of British Columbia, Vancouver, BC, Canada, V6T 1Z1
b Department of Plant Biology, Cornell University, Ithaca, New York 14853
AuthorAffiliation_xml – name: c Department of Chemistry, University of British Columbia, Vancouver, BC, Canada, V6T 1Z1
– name: a Department of Botany, University of British Columbia, Vancouver, BC, Canada V6T 1Z4
– name: b Department of Plant Biology, Cornell University, Ithaca, New York 14853
Author_xml – sequence: 1
  fullname: DeBono, Allan
– sequence: 2
  fullname: Yeats, Trevor H
– sequence: 3
  fullname: Rose, Jocelyn K.C
– sequence: 4
  fullname: Bird, David
– sequence: 5
  fullname: Jetter, Reinhard
– sequence: 6
  fullname: Kunst, Ljerka
– sequence: 7
  fullname: Samuels, Lacey
BackLink https://www.ncbi.nlm.nih.gov/pubmed/19366900$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright Copyright 2009 American Society of Plant Biologists
Copyright American Society of Plant Biologists Apr 2009
Copyright © 2009, American Society of Plant Biologists
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– notice: Copyright American Society of Plant Biologists Apr 2009
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Online version contains Web-only data.
Address correspondence to lsamuels@interchange.ubc.ca.
The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantcell.org) is: Lacey Samuels (lsamuels@interchange.ubc.ca).
Open Access articles can be viewed online without a subscription.
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Snippet 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...
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....
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StartPage 1230
SubjectTerms Animal cuticle
Arabidopsis - metabolism
Arabidopsis - ultrastructure
Arabidopsis Proteins - analysis
Arabidopsis Proteins - metabolism
Arabidopsis Proteins - physiology
Carrier Proteins - analysis
Carrier Proteins - metabolism
Carrier Proteins - physiology
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cell walls
Epicuticular wax
Epidermal cells
Fluorescence
Glycosylphosphatidylinositols - metabolism
Lipid Metabolism - physiology
Lipids
Luminescent Proteins - analysis
Mutation
Phenotype
Plant cells
Plant cuticle
Plant Stems - metabolism
Plants
Promoter Regions, Genetic
Waxes
Waxes - metabolism
Title Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface
URI https://www.jstor.org/stable/40536876
https://www.ncbi.nlm.nih.gov/pubmed/19366900
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