Source:http://linkedlifedata.com/resource/pubmed/id/17971043
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-1-10
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pubmed:abstractText |
The gravitropism defective 2 (grv2) mutants of Arabidopsis thaliana were previously characterized as exhibiting shoot agravitropism resulting from mutations in a homolog of the Caenorhabditis elegans RECEPTOR-MEDIATED ENDOCYTOSIS-8 (RME-8) gene, which is required in C. elegans for endocytosis. A fluorescent protein fusion to the GRV2 protein localized to endosomes in transgenic plants, and vacuolar morphology was altered in grv2 mutants. A defect in vacuolar membrane dynamics provides a mechanistic explanation for the gravitropic defect, and may also account for the presence of an enlarged vacuole in early embryos, together with a nutrient requirement during seedling establishment. The GRV2-positive endosomes were sensitive to Wortmannin but not brefeldin A (BFA), consistent with GRV2 operating late in the endocytic pathway, prior to delivery of vesicles to the central vacuole. The specific enlargement of GRV2:YFP structures by Wortmannin, together with biochemical data showing that GRV2 co-fractionates with pre-vacuolar markers such as PEP12/SYP21, leads us to conclude that in plants GRV2/RME-8 functions in vesicle trafficking from the multivesicular body/pre-vacuolar compartment to the lytic vacuole.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KAM2 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Rme-8 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29-41
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pubmed:meshHeading |
pubmed-meshheading:17971043-Androstadienes,
pubmed-meshheading:17971043-Animals,
pubmed-meshheading:17971043-Arabidopsis,
pubmed-meshheading:17971043-Arabidopsis Proteins,
pubmed-meshheading:17971043-Brefeldin A,
pubmed-meshheading:17971043-Caenorhabditis elegans,
pubmed-meshheading:17971043-Drosophila Proteins,
pubmed-meshheading:17971043-Endocytosis,
pubmed-meshheading:17971043-Endosomes,
pubmed-meshheading:17971043-Gravitropism,
pubmed-meshheading:17971043-Intracellular Membranes,
pubmed-meshheading:17971043-Mutation,
pubmed-meshheading:17971043-Vacuoles,
pubmed-meshheading:17971043-Vesicular Transport Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
The GRV2/RME-8 protein of Arabidopsis functions in the late endocytic pathway and is required for vacuolar membrane flow.
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pubmed:affiliation |
Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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