Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-9-24
pubmed:abstractText
In plants, cell polarity and tissue patterning are connected by intercellular flow of the phytohormone auxin, whose directional signaling depends on polar subcellular localization of PIN auxin transport proteins. The mechanism of polar targeting of PINs or other cargos in plants is largely unidentified, with the PINOID kinase being the only known molecular component. Here, we identify PP2A phosphatase as an important regulator of PIN apical-basal targeting and auxin distribution. Genetic analysis, localization, and phosphorylation studies demonstrate that PP2A and PINOID both partially colocalize with PINs and act antagonistically on the phosphorylation state of their central hydrophilic loop, hence mediating PIN apical-basal polar targeting. Thus, in plants, polar sorting by the reversible phosphorylation of cargos allows for their conditional delivery to specific intracellular destinations. In the case of PIN proteins, this mechanism enables switches in the direction of intercellular auxin fluxes, which mediate differential growth, tissue patterning, and organogenesis.
pubmed:grant
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/Indoleacetic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PIN1 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/PIN2 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/PIN4 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/PINOID protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion 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
1044-56
pubmed:dateRevised
2011-4-6
pubmed:meshHeading
pubmed-meshheading:17889649-Arabidopsis, pubmed-meshheading:17889649-Arabidopsis Proteins, pubmed-meshheading:17889649-Cell Polarity, pubmed-meshheading:17889649-Endosomes, pubmed-meshheading:17889649-Genotype, pubmed-meshheading:17889649-Indoleacetic Acids, pubmed-meshheading:17889649-Membrane Transport Proteins, pubmed-meshheading:17889649-Meristem, pubmed-meshheading:17889649-Mutation, pubmed-meshheading:17889649-Phenotype, pubmed-meshheading:17889649-Phosphoprotein Phosphatases, pubmed-meshheading:17889649-Phosphorylation, pubmed-meshheading:17889649-Plants, Genetically Modified, pubmed-meshheading:17889649-Protein Subunits, pubmed-meshheading:17889649-Protein Transport, pubmed-meshheading:17889649-Protein-Serine-Threonine Kinases, pubmed-meshheading:17889649-Recombinant Fusion Proteins, pubmed-meshheading:17889649-Seedling, pubmed-meshheading:17889649-Signal Transduction
pubmed:year
2007
pubmed:articleTitle
Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux.
pubmed:affiliation
Zentrum für Molekularbiologie der Pflanzen, Universität Tübingen, Tübingen, Germany.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't