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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
36
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pubmed:dateCreated |
2003-9-1
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pubmed:abstractText |
The plant hormone ethylene is perceived by a five-member family of receptors related to the bacterial histidine kinases. The Raf-like kinase CTR1 functions downstream of the ethylene receptors as a negative regulator of ethylene signal transduction. CTR1 is shown here to be associated with membranes of the endoplasmic reticulum in Arabidopsis as a result of its interactions with ethylene receptors. Membrane association of CTR1 is reduced by mutations that eliminate ethylene receptors and by a mutation in CTR1 that reduces its ability to bind to the ethylene receptor ETR1. Direct evidence that CTR1 is part of an ethylene receptor signaling complex was obtained by co-purification of the ethylene receptor ETR1 with a tagged version of CTR1 from an Arabidopsis membrane extract. The histidine kinase activity of ETR1 is not required for its association with CTR1, based on co-purification of tagged ETR1 mutants and CTR1 after expression in a transgenic yeast system. These data demonstrate that CTR1 is part of an ethylene receptor signaling complex in Arabidopsis and support a model in which localization of CTR1 to the endoplasmic reticulum is necessary for its function. Additional data that demonstrate a post-transcriptional effect of ethylene upon the expression of CTR1 suggest that production of ethylene receptor signaling complexes may be coordinately regulated.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CTR1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sucrose,
http://linkedlifedata.com/resource/pubmed/chemical/ethylene receptors, plant
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34725-32
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pubmed:dateRevised |
2010-1-15
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pubmed:meshHeading |
pubmed-meshheading:12821658-Arabidopsis,
pubmed-meshheading:12821658-Blotting, Northern,
pubmed-meshheading:12821658-Cell Membrane,
pubmed-meshheading:12821658-Centrifugation, Density Gradient,
pubmed-meshheading:12821658-Endoplasmic Reticulum,
pubmed-meshheading:12821658-Glutathione Transferase,
pubmed-meshheading:12821658-Immunoblotting,
pubmed-meshheading:12821658-Microsomes,
pubmed-meshheading:12821658-Models, Biological,
pubmed-meshheading:12821658-Mutation,
pubmed-meshheading:12821658-Plant Proteins,
pubmed-meshheading:12821658-Protein Binding,
pubmed-meshheading:12821658-Protein Kinases,
pubmed-meshheading:12821658-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:12821658-RNA,
pubmed-meshheading:12821658-Receptors, Cell Surface,
pubmed-meshheading:12821658-Recombinant Fusion Proteins,
pubmed-meshheading:12821658-Signal Transduction,
pubmed-meshheading:12821658-Sucrose,
pubmed-meshheading:12821658-Time Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Localization of the Raf-like kinase CTR1 to the endoplasmic reticulum of Arabidopsis through participation in ethylene receptor signaling complexes.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of New Hampshire, Durham, New Hampshire 03824, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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