ArticleThe Plant cell2023
The START domain potentiates HD-ZIPIII transcriptional activity.
Article in The Plant cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A cryptic START domain regulates deeply conserved transcription factors.The Plant cell · 2026Article
- Altered Meristem Initiation Is Associated with IncreasedBiology · 2026Article
- Getting a grip on StAR-related lipid-transfer (START) domain proteins in bacteria.FEMS microbiology reviews · 2026Review
- From binding to networks: methods for identifying transcription factor targets in plant systems.Frontiers in plant science · 2026Review
- Evolutionary Diversification and Adaptive Evolution Analysis of the Plant HD-Zip IV Subfamily.Genes · 2025Article
- A bHLH7-PDF2 module mediates transcriptional regulation to repress seed oil accumulation in Arabidopsis thaliana.Plant communications · 2025Article
- START domains generate paralog-specific regulons from a single network architecture.Nature communications · 2024Article
- Arabidopsis PROTODERMAL FACTOR2 binds lysophosphatidylcholines and transcriptionally regulates phospholipid metabolism.The New phytologist · 2024Article
- The Ins and Outs of Homeodomain-Leucine Zipper/Hormone Networks in the Regulation of Plant Development.International journal of molecular sciences · 2024Review
- HD-Zip IV transcription factors: Drivers of epidermal cell fate integrate metabolic signals.Current opinion in plant biology · 2023Review
- A conserved mechanism determines the activity of two pivotal transcription factors that control epidermal cell differentiation in Arabidopsis thaliana.Journal of plant research · 2023Article
- Cavity architecture based modulation of ligand binding tunnels in plant START domains.Computational and structural biotechnology journal · 2023Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CLASS III HOMEODOMAIN-LEUCINE ZIPPER (HD-ZIPIII) transcription factors (TFs) were repeatedly deployed over 725 million years of evolution to regulate central developmental innovations. The START domain of this pivotal class of developmental regulators was recognized over 20 years ago, but its putative ligands and functional contributions remain unknown. Here, we demonstrate that the START domain promotes HD-ZIPIII TF homodimerization and increases transcriptional potency. Effects on transcriptional output can be ported onto heterologous TFs, consistent with principles of evolution via domain capture. We also show the START domain binds several species of phospholipids, and that mutations in conserved residues perturbing ligand binding and/or its downstream conformational readout abolish HD-ZIPIII DNA-binding competence. Our data present a model in which the START domain potentiates transcriptional activity and uses ligand-induced conformational change to render HD-ZIPIII dimers competent to bind DNA. These findings resolve a long-standing mystery in plant development and highlight the flexible and diverse regulatory potential coded within this widely distributed evolutionary module.
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