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The F-box protein TIR1 is an auxin receptor

The plant hormone auxin regulates diverse aspects of plant growth and development. Recent studies indicate that auxin acts by promoting the degradation of the Aux/IAA transcriptional repressors through the action of the ubiquitin protein ligase SCF(TIR1). The nature of the signalling cascade that le... Full description

Journal Title: Nature 2005-05-26, Vol.435 (7041), p.441-445
Main Author: Dharmasiri, Nihal
Other Authors: Dharmasiri, Sunethra , Estelle, Mark
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: London: Nature Publishing
ID: ISSN: 0028-0836
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recordid: cdi_proquest_miscellaneous_743502703
title: The F-box protein TIR1 is an auxin receptor
format: Article
creator:
  • Dharmasiri, Nihal
  • Dharmasiri, Sunethra
  • Estelle, Mark
subjects:
  • Amino Acid Sequence
  • Animals
  • Arabidopsis - genetics
  • Arabidopsis - metabolism
  • Arabidopsis Proteins - chemistry
  • Arabidopsis Proteins - genetics
  • Arabidopsis Proteins - isolation & purification
  • Arabidopsis Proteins - metabolism
  • Biological and medical sciences
  • Carrier Proteins - chemistry
  • Carrier Proteins - genetics
  • Carrier Proteins - isolation & purification
  • Carrier Proteins - metabolism
  • Cell Line
  • DNA-Binding Proteins - metabolism
  • F-Box Proteins - chemistry
  • F-Box Proteins - genetics
  • F-Box Proteins - isolation & purification
  • F-Box Proteins - metabolism
  • Fundamental and applied biological sciences. Psychology
  • Gene Expression Regulation, Plant - drug effects
  • Growth regulators
  • Indoleacetic Acids - metabolism
  • Indoleacetic Acids - pharmacology
  • Metabolism
  • Molecular Sequence Data
  • Nuclear Proteins - metabolism
  • Plant physiology and development
  • Protein Binding - drug effects
  • Receptors, Cell Surface - chemistry
  • Receptors, Cell Surface - genetics
  • Receptors, Cell Surface - isolation & purification
  • Receptors, Cell Surface - metabolism
  • Repressor Proteins - metabolism
  • Signal Transduction
  • SKP Cullin F-Box Protein Ligases - chemistry
  • SKP Cullin F-Box Protein Ligases - metabolism
  • Space life sciences
  • Spodoptera
  • Temperature
  • Transcription, Genetic - drug effects
ispartof: Nature, 2005-05-26, Vol.435 (7041), p.441-445
description: The plant hormone auxin regulates diverse aspects of plant growth and development. Recent studies indicate that auxin acts by promoting the degradation of the Aux/IAA transcriptional repressors through the action of the ubiquitin protein ligase SCF(TIR1). The nature of the signalling cascade that leads to this effect is not known. However, recent studies indicate that the auxin receptor and other signalling components involved in this response are soluble factors. Using an in vitro pull-down assay, we demonstrate that the interaction between transport inhibitor response 1 (TIR1) and Aux/IAA proteins does not require stable modification of either protein. Instead auxin promotes the Aux/IAA-SCF(TIR1) interaction by binding directly to SCF(TIR1). We further show that the loss of TIR1 and three related F-box proteins eliminates saturable auxin binding in plant extracts. Finally, TIR1 synthesized in insect cells binds Aux/IAA proteins in an auxin-dependent manner. Together, these results indicate that TIR1 is an auxin receptor that mediates Aux/IAA degradation and auxin-regulated transcription.
language: eng
source:
identifier: ISSN: 0028-0836
fulltext: no_fulltext
issn:
  • 0028-0836
  • 1476-4687
url: Link


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titleThe F-box protein TIR1 is an auxin receptor
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descriptionThe plant hormone auxin regulates diverse aspects of plant growth and development. Recent studies indicate that auxin acts by promoting the degradation of the Aux/IAA transcriptional repressors through the action of the ubiquitin protein ligase SCF(TIR1). The nature of the signalling cascade that leads to this effect is not known. However, recent studies indicate that the auxin receptor and other signalling components involved in this response are soluble factors. Using an in vitro pull-down assay, we demonstrate that the interaction between transport inhibitor response 1 (TIR1) and Aux/IAA proteins does not require stable modification of either protein. Instead auxin promotes the Aux/IAA-SCF(TIR1) interaction by binding directly to SCF(TIR1). We further show that the loss of TIR1 and three related F-box proteins eliminates saturable auxin binding in plant extracts. Finally, TIR1 synthesized in insect cells binds Aux/IAA proteins in an auxin-dependent manner. Together, these results indicate that TIR1 is an auxin receptor that mediates Aux/IAA degradation and auxin-regulated transcription.
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languageeng
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subjectAmino Acid Sequence ; Animals ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - isolation & purification ; Arabidopsis Proteins - metabolism ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Cell Line ; DNA-Binding Proteins - metabolism ; F-Box Proteins - chemistry ; F-Box Proteins - genetics ; F-Box Proteins - isolation & purification ; F-Box Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Plant - drug effects ; Growth regulators ; Indoleacetic Acids - metabolism ; Indoleacetic Acids - pharmacology ; Metabolism ; Molecular Sequence Data ; Nuclear Proteins - metabolism ; Plant physiology and development ; Protein Binding - drug effects ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - genetics ; Receptors, Cell Surface - isolation & purification ; Receptors, Cell Surface - metabolism ; Repressor Proteins - metabolism ; Signal Transduction ; SKP Cullin F-Box Protein Ligases - chemistry ; SKP Cullin F-Box Protein Ligases - metabolism ; Space life sciences ; Spodoptera ; Temperature ; Transcription, Genetic - drug effects
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descriptionThe plant hormone auxin regulates diverse aspects of plant growth and development. Recent studies indicate that auxin acts by promoting the degradation of the Aux/IAA transcriptional repressors through the action of the ubiquitin protein ligase SCF(TIR1). The nature of the signalling cascade that leads to this effect is not known. However, recent studies indicate that the auxin receptor and other signalling components involved in this response are soluble factors. Using an in vitro pull-down assay, we demonstrate that the interaction between transport inhibitor response 1 (TIR1) and Aux/IAA proteins does not require stable modification of either protein. Instead auxin promotes the Aux/IAA-SCF(TIR1) interaction by binding directly to SCF(TIR1). We further show that the loss of TIR1 and three related F-box proteins eliminates saturable auxin binding in plant extracts. Finally, TIR1 synthesized in insect cells binds Aux/IAA proteins in an auxin-dependent manner. Together, these results indicate that TIR1 is an auxin receptor that mediates Aux/IAA degradation and auxin-regulated transcription.
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3Arabidopsis - metabolism
4Arabidopsis Proteins - chemistry
5Arabidopsis Proteins - genetics
6Arabidopsis Proteins - isolation & purification
7Arabidopsis Proteins - metabolism
8Biological and medical sciences
9Carrier Proteins - chemistry
10Carrier Proteins - genetics
11Carrier Proteins - isolation & purification
12Carrier Proteins - metabolism
13Cell Line
14DNA-Binding Proteins - metabolism
15F-Box Proteins - chemistry
16F-Box Proteins - genetics
17F-Box Proteins - isolation & purification
18F-Box Proteins - metabolism
19Fundamental and applied biological sciences. Psychology
20Gene Expression Regulation, Plant - drug effects
21Growth regulators
22Indoleacetic Acids - metabolism
23Indoleacetic Acids - pharmacology
24Metabolism
25Molecular Sequence Data
26Nuclear Proteins - metabolism
27Plant physiology and development
28Protein Binding - drug effects
29Receptors, Cell Surface - chemistry
30Receptors, Cell Surface - genetics
31Receptors, Cell Surface - isolation & purification
32Receptors, Cell Surface - metabolism
33Repressor Proteins - metabolism
34Signal Transduction
35SKP Cullin F-Box Protein Ligases - chemistry
36SKP Cullin F-Box Protein Ligases - metabolism
37Space life sciences
38Spodoptera
39Temperature
40Transcription, Genetic - drug effects
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28Protein Binding - drug effects
29Receptors, Cell Surface - chemistry
30Receptors, Cell Surface - genetics
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32Receptors, Cell Surface - metabolism
33Repressor Proteins - metabolism
34Signal Transduction
35SKP Cullin F-Box Protein Ligases - chemistry
36SKP Cullin F-Box Protein Ligases - metabolism
37Space life sciences
38Spodoptera
39Temperature
40Transcription, Genetic - drug effects
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abstractThe plant hormone auxin regulates diverse aspects of plant growth and development. Recent studies indicate that auxin acts by promoting the degradation of the Aux/IAA transcriptional repressors through the action of the ubiquitin protein ligase SCF(TIR1). The nature of the signalling cascade that leads to this effect is not known. However, recent studies indicate that the auxin receptor and other signalling components involved in this response are soluble factors. Using an in vitro pull-down assay, we demonstrate that the interaction between transport inhibitor response 1 (TIR1) and Aux/IAA proteins does not require stable modification of either protein. Instead auxin promotes the Aux/IAA-SCF(TIR1) interaction by binding directly to SCF(TIR1). We further show that the loss of TIR1 and three related F-box proteins eliminates saturable auxin binding in plant extracts. Finally, TIR1 synthesized in insect cells binds Aux/IAA proteins in an auxin-dependent manner. Together, these results indicate that TIR1 is an auxin receptor that mediates Aux/IAA degradation and auxin-regulated transcription.
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