ArticleThe Plant cell2001
Rapid degradation of auxin/indoleacetic acid proteins requires conserved amino acids of domain II and is proteasome dependent.
Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.
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Who cites it
145 citing papers in PubMed, 324 citations in OpenAlex.
- Deciphering resistance mechanisms to auxin-inducible protein degradation in mammalian cells.The Journal of biological chemistry · 2026Article
- Salicylic acid modulates its catabolic enzymes via proteasomal degradation linked to SCF-associated proximity networks.Nature communications · 2026Article
- Genome-Wide Identification and Expression Profiling of theInternational journal of molecular sciences · 2025Article
- Aux/IAAs: specificity and redundancy.Plant signaling & behavior · 2025Review
- Mechanisms of auxin action in plant growth and development.Nature reviews. Molecular cell biology · 2025Review
- Core biological principles and tools stemming from basic Arabidopsis research.The Plant cell · 2025Review
- Stochastic gene expression in auxin signaling in the floral meristem of Arabidopsis thaliana.Nature communications · 2025Article
- Genome-Wide Identification and Expression Analysis of the Aux/IAA Gene Family in Lettuce (International journal of molecular sciences · 2025Article
- A single-nucleotide mutation of G301A inFrontiers in plant science · 2025Article
- DRMY1 promotes robust morphogenesis in Arabidopsis by sustaining the translation of cytokinin-signaling inhibitor proteins.Developmental cell · 2024Article
- Protein degradation in auxin response.The Plant cell · 2024Review
- A point mutation in thePhysiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- WAV E3 ubiquitin ligases mediate degradation of IAA32/34 in the TMK1-mediated auxin signaling pathway during apical hook development.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Large-scale analysis of the ARF and Aux/IAA gene families in 406 horticultural and other plants.Molecular horticulture · 2024Article
- Article
- Identification of potential auxin response candidate genes for soybean rapid canopy coverage through comparative evolution and expression analysis.Frontiers in plant science · 2024Article
- A non-canonicalFrontiers in plant science · 2024Article
- Identification of potential Auxin Response Candidate genes for soybean rapid canopy coverage through comparative evolution and expression analysis.bioRxiv : the preprint server for biology · 2023Article
- Intrinsic disorder and conformational coexistence in auxin coreceptors.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A New Function ofPlants (Basel, Switzerland) · 2023Article
85 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Auxin rapidly induces auxin/indoleacetic acid (Aux/IAA) transcription. The proteins encoded are short-lived nucleus-localized transcriptional regulators that share four conserved domains. In a transient assay measuring protein accumulation, an Aux/IAA 13-amino acid domain II consensus sequence was sufficient to target firefly luciferase (LUC) for low protein accumulation equivalent to that observed previously for full-length PSIAA6. Single amino acid substitutions in these 13 amino acids, corresponding to known auxin response mutants, resulted in a sixfold to 20-fold increase in protein accumulation. Naturally occurring variant amino acids had no effect. Residues identified as essential by single alanine substitutions were not sufficient when all flanking amino acids were alanine, indicating the importance of flanking regions. Using direct protein degradation measurements in transgenic Arabidopsis seedlings, full-length IAA1, PSIAA6, and the N-terminal 73 PSIAA6 amino acids targeted LUC for rapid degradation with 8-min half-lives. The C-terminal 109 amino acids did not affect LUC half-life. Smaller regions containing domain II also targeted LUC for rapid degradation, but the rates were not equivalent to those of the full-length protein. A single domain II substitution in the context of full-length PSIAA6 increased half-life 30-fold. Proteasome inhibitors affected Aux/IAA::LUC fusion protein accumulation, demonstrating the involvement of the proteasome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.