Localization of the Raf-like kinase CTR1 to the endoplasmic reticulum of Arabidopsis through participation in ethylene receptor signaling complexes.
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.
Mesh Terms:
Arabidopsis, Blotting, Northern, Cell Membrane, Centrifugation, Density Gradient, Endoplasmic Reticulum, Glutathione Transferase, Immunoblotting, Microsomes, Models, Biological, Mutation, Plant Proteins, Protein Binding, Protein Kinases, Proto-Oncogene Proteins c-raf, RNA, Receptors, Cell Surface, Recombinant Fusion Proteins, Signal Transduction, Sucrose, Time Factors
Arabidopsis, Blotting, Northern, Cell Membrane, Centrifugation, Density Gradient, Endoplasmic Reticulum, Glutathione Transferase, Immunoblotting, Microsomes, Models, Biological, Mutation, Plant Proteins, Protein Binding, Protein Kinases, Proto-Oncogene Proteins c-raf, RNA, Receptors, Cell Surface, Recombinant Fusion Proteins, Signal Transduction, Sucrose, Time Factors
J. Biol. Chem.
Date: Sep. 05, 2003
PubMed ID: 12821658
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