Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-9-24
pubmed:abstractText
A key feature of plants (as opposed to animals) is their ability to establish new organs not only during embryogenesis, but also throughout their development. A master regulator of organ initiation in plants is the phytohormone auxin. Auxin acts locally as a morphogen and is directionally transported from cell to cell by polarized auxin efflux carriers, termed PIN-FORMED (PIN) proteins. Here we report that the Arabidopsis ortholog of the yeast and mammalian vacuolar protein sorting 29 (VPS29), a member of the retromer complex, mediates the formation of new axes of development. Furthermore, we show that VPS29 is required for endosome homeostasis, PIN protein cycling, and dynamic PIN1 repolarization during development. We propose a model that links VPS29 function, PIN1 polarity, and organ initiation in plants.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GNOM protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors, http://linkedlifedata.com/resource/pubmed/chemical/Indoleacetic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Mag1 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/PIN1 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/PIN2 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sorting Nexins, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
130
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1057-70
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:17889650-Arabidopsis, pubmed-meshheading:17889650-Arabidopsis Proteins, pubmed-meshheading:17889650-Carrier Proteins, pubmed-meshheading:17889650-Cell Differentiation, pubmed-meshheading:17889650-Cell Polarity, pubmed-meshheading:17889650-Cell Proliferation, pubmed-meshheading:17889650-Cotyledon, pubmed-meshheading:17889650-Endosomes, pubmed-meshheading:17889650-Genotype, pubmed-meshheading:17889650-Guanine Nucleotide Exchange Factors, pubmed-meshheading:17889650-Indoleacetic Acids, pubmed-meshheading:17889650-Membrane Transport Proteins, pubmed-meshheading:17889650-Meristem, pubmed-meshheading:17889650-Multiprotein Complexes, pubmed-meshheading:17889650-Mutation, pubmed-meshheading:17889650-Phenotype, pubmed-meshheading:17889650-Plants, Genetically Modified, pubmed-meshheading:17889650-Protein Transport, pubmed-meshheading:17889650-Recombinant Fusion Proteins, pubmed-meshheading:17889650-Signal Transduction, pubmed-meshheading:17889650-Sorting Nexins, pubmed-meshheading:17889650-Vesicular Transport Proteins, pubmed-meshheading:17889650-Xylem
pubmed:year
2007
pubmed:articleTitle
The retromer protein VPS29 links cell polarity and organ initiation in plants.
pubmed:affiliation
Reproduction et Développement des Plantes, Institut Fédératif de Recherche 128, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Université Claude Bernard Lyon I, Ecole Normale Supérieure de Lyon, Lyon, France.
pubmed:publicationType
Journal Article