ARF-Aux/IAA interactions through domain III/IV are not strictly required for auxin-responsive gene expression

Wang, Shucai; Hagen, Gretchen; Guilfoyle, Tom J.

doi:10.4161/psb.24526

Cited by 20 publications

(19 citation statements)

References 27 publications

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“…5)-an idea supported by the assorted interactions between ARF and Aux/IAA proteins (15). Further, because ARF C termini are unnecessary for ARF transcriptional activity (27), our results provide a specific function for ARF and Aux/IAA PB1 domains.…”

Section: Discussionsupporting

confidence: 49%

Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression

Korasick

Westfall

Lee

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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254

279

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In plants, the AUXIN RESPONSE FACTOR (ARF) transcription factor family regulates gene expression in response to auxin. In the absence of auxin, ARF transcription factors are repressed by interaction with AUXIN/INDOLE 3-ACETIC ACID (Aux/IAA) proteins. Although the C termini of ARF and Aux/IAA proteins facilitate their homo-and heterooligomerization, the molecular basis for this interaction remained undefined. The crystal structure of the C-terminal interaction domain of Arabidopsis ARF7 reveals a Phox and Bem1p (PB1) domain that provides both positive and negative electrostatic interfaces for directional protein interaction. Mutation of interface residues in the ARF7 PB1 domain yields monomeric protein and abolishes interaction with both itself and IAA17. Expression of a stabilized Aux/IAA protein (i.e., IAA16) bearing PB1 mutations in Arabidopsis suggests a multimerization requirement for ARF protein repression, leading to a refined auxinsignaling model.

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Section: Discussionsupporting

confidence: 49%

Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression

Korasick

Westfall

Lee

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

254

279

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“…Mutational analysis and small-angle X-ray scattering (SAXS) experiments verify that ARF DBD dimerization occurs in solution and is important in planta for transcriptional activity [34], as previously suggested [12]. Indeed, earlier domain deletion experiments are consistent with the dimeric ARF DBD structures [35–37]. …”

Section: Mechanistic Clues Of Auxin Responsive Gene Transcription Thrsupporting

confidence: 71%

Refining the nuclear auxin response pathway through structural biology

Korasick

Jez

Strader

2015

Current Opinion in Plant Biology

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Auxin is a key regulator of plant growth and development. Classical molecular and genetic techniques employed over the past 20 years identified the major players in auxin-mediated gene expression and suggest a canonical auxin response pathway. In recent years, structural and biophysical studies clarified the molecular details of auxin perception, the recognition of DNA by auxin transcription factors, and the interaction of auxin transcription factors with repressor proteins. These studies refine the auxin signal transduction model and raise new questions that increase the complexity of auxin signaling.

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“…However, activators ARF5 and ARF7 without a PB1 domain are still responsive to auxin in protoplast transfection assays in the arf7 background, although at a lower level than full‐length ARF5 and ARF7 proteins (Wang et al . ), showing that for these ARFs, the PB1 domain is not essential for auxin response. For ARF5, the auxin response was also independent of whether the DBD was derived from an activating ARF (ARF6 or ARF7) or repressor ARF (ARF1) (Wang et al .…”

Section: Irrepressible Auxin Response Factorsmentioning

confidence: 97%

Auxin response factors

Chandler

2016

Plant Cell & Environment

237

188

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Auxin signalling involves the activation or repression of gene expression by a class of auxin response factor (ARF) proteins that bind to auxin response elements in auxin-responsive gene promoters. The release of ARF repression in the presence of auxin by the degradation of their cognate auxin/indole-3-acetic acid repressors forms a paradigm of transcriptional response to auxin. However, this mechanism only applies to activating ARFs, and further layers of complexity of ARF function and regulation are being revealed, which partly reflect their highly modular domain structure. This review summarizes our knowledge concerning ARF binding site specificity, homodimer and heterodimer multimeric ARF association and cooperative function and how activator ARFs activate target genes via chromatin remodelling and evolutionary information derived from phylogenetic comparisons from ARFs from diverse species. ARFs are regulated in diverse ways, and their importance in non-auxin-regulated pathways is becoming evident. They are also embedded within higher-order transcription factor complexes that integrate signalling pathways from other hormones and in response to the environment. The ways in which new information concerning ARFs on many levels is causing a revision of existing paradigms of auxin response are discussed.

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ARF-Aux/IAA interactions through domain III/IV are not strictly required for auxin-responsive gene expression

Cited by 20 publications

References 27 publications

Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression

Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression

Refining the nuclear auxin response pathway through structural biology

Auxin response factors

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