title: A member of the PLEIOTROPIC DRUG RESISTANCE family of ATP binding cassette transporters is required for the formation of a functional cuticle in Arabidopsis.
abstract: Although the multilayered structure of the plant cuticle was discovered many years ago, the molecular basis of its formation and the functional relevance of the layers are not understood. Here, we present the permeable cuticle1 (pec1) mutant of Arabidopsis thaliana, which displays features associated with a highly permeable cuticle in several organs. In pec1 flowers, typical cutin monomers, such as ω-hydroxylated fatty acids and 10,16-dihydroxypalmitate, are reduced to 40% of wild-type levels and are accompanied by the appearance of lipidic inclusions within the epidermal cell. The cuticular layer of the cell wall, rather than the cuticle proper, is structurally altered in pec1 petals. Therefore, a significant role for the formation of the diffusion barrier in petals can be attributed to this layer. Thus, pec1 defines a new class of mutants. The phenotypes of the pec1 mutant are caused by the knockout of ATP BINDING CASSETTEG32 (ABCG32), an ABC transporter from the PLEIOTROPIC DRUG RESISTANCE family that is localized at the plasma membrane of epidermal cells in a polar manner toward the surface of the organs. Our results suggest that ABCG32 is involved in the formation of the cuticular layer of the cell wall, most likely by exporting particular cutin precursors from the epidermal cell.
authors.affiliation: Department of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland.
authors.forename: Michael
authors.initials: M
authors.lastname: Bessire
authors.forename: Sandra
authors.initials: S
authors.lastname: Borel
authors.forename: Guillaume
authors.initials: G
authors.lastname: Fabre
authors.forename: Luis
authors.initials: L
authors.lastname: Carraça
authors.forename: Nadia
authors.initials: N
authors.lastname: Efremova
authors.forename: Alexander
authors.initials: A
authors.lastname: Yephremov
authors.forename: Yan
authors.initials: Y
authors.lastname: Cao
authors.forename: Reinhard
authors.initials: R
authors.lastname: Jetter
authors.forename: Anne-Claude
authors.initials: AC
authors.lastname: Jacquat
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Métraux
authors.forename: Christiane
authors.initials: C
authors.lastname: Nawrath
mesh_terms: D064286:ATP Binding Cassette Transporter 1; D000070996:ATP Binding Cassette Transporter, Subfamily G; D018528:ATP-Binding Cassette Transporters / Q000235:genetics / Q000378:metabolism*; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane; D002473:Cell Wall / Q000378:metabolism; D035264:Flowers / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D018506:Gene Expression Regulation, Plant; D005838:Genotype; D008563:Membrane Lipids / Q000378:metabolism*; D010539:Permeability; D010641:Phenotype; D019441:Plant Epidermis / Q000378:metabolism*; D018515:Plant Leaves / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion
chemical_list: C577839:ABCG32 protein, Arabidopsis; D064286:ATP Binding Cassette Transporter 1; D000070996:ATP Binding Cassette Transporter, Subfamily G; D018528:ATP-Binding Cassette Transporters; D029681:Arabidopsis Proteins; D008563:Membrane Lipids; C000521:cutin