ArticleGenome biology2004
START lipid/sterol-binding domains are amplified in plants and are predominantly associated with homeodomain transcription factors.
Article in Genome biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.
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Who cites it
134 citing papers in PubMed, 288 citations in OpenAlex.
- A cryptic START domain regulates deeply conserved transcription factors.The Plant cell · 2026Article
- Domain architecture of plant eukaryotic translation initiation factor 3 subunit E governs interaction with translational cis-elements to regulatepollen tube growth.The Plant cell · 2026Article
- Article
- Genome-wide association study of exotic Fragaria germplasm accessions for resistance to Phytophthora crown rot in strawberry.BMC plant biology · 2026Article
- Getting a grip on StAR-related lipid-transfer (START) domain proteins in bacteria.FEMS microbiology reviews · 2026Review
- Genome-wide identification of theFrontiers in plant science · 2026Article
- Evolutionary Diversification and Adaptive Evolution Analysis of the Plant HD-Zip IV Subfamily.Genes · 2025Article
- CottonGenes · 2025Article
- Domain characteristics, classification and expression profiles in response to various abiotic stresses of four HD-Zip subfamilies in tea plant.BMC plant biology · 2025Article
- Sterols in plant biologyCell surface (Amsterdam, Netherlands) · 2025Review
- Review
- ChREBP-mediated up-regulation of Them1 coordinates thermogenesis with glycolysis and lipogenesis in response to chronic stress.Science signaling · 2024Article
- 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
- Phosphatidylcholine Transfer Protein OsPCTP Interacts with Ascorbate Peroxidase OsAPX8 to Regulate Bacterial Blight Resistance in Rice.International journal of molecular sciences · 2024Article
- Structure, function, and lipid sensing activity in the thioesterase superfamily.Biochemical Society transactions · 2024Review
- Genome-Wide Identification, Characterization, and Expression Analysis of the HD-Zip Gene Family inGenes · 2024Article
- Genome-wide characterization and expression profiling of the HD-ZIP gene family in Acoraceae under salinity and cold stress.Frontiers in plant science · 2024Article
- High-throughput screening identifies small molecule inhibitors of thioesterase superfamily member 1: Implications for the management of non-alcoholic fatty liver disease.Molecular metabolism · 2023Article
- HD-Zip IV transcription factors: Drivers of epidermal cell fate integrate metabolic signals.Current opinion in plant biology · 2023Review
74 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
backgroundIn animals, steroid hormones regulate gene expression by binding to nuclear receptors. Plants lack genes for nuclear receptors, yet genetic evidence from Arabidopsis suggests developmental roles for lipids/sterols analogous to those in animals. In contrast to nuclear receptors, the lipid/sterol-binding StAR-related lipid transfer (START) protein domains are conserved, making them candidates for involvement in both animal and plant lipid/sterol signal transduction.
resultsWe surveyed putative START domains from the genomes of Arabidopsis, rice, animals, protists and bacteria. START domains are more common in plants than in animals and in plants are primarily found within homeodomain (HD) transcription factors. The largest subfamily of HD-START proteins is characterized by an HD amino-terminal to a plant-specific leucine zipper with an internal loop, whereas in a smaller subfamily the HD precedes a classic leucine zipper. The START domains in plant HD-START proteins are not closely related to those of animals, implying collateral evolution to accommodate organism-specific lipids/sterols. Using crystal structures of mammalian START proteins, we show structural conservation of the mammalian phosphatidylcholine transfer protein (PCTP) START domain in plants, consistent with a common role in lipid transport and metabolism. We also describe putative START-domain proteins from bacteria and unicellular protists.
conclusionsThe majority of START domains in plants belong to a novel class of putative lipid/sterol-binding transcription factors, the HD-START family, which is conserved across the plant kingdom. HD-START proteins are confined to plants, suggesting a mechanism by which lipid/sterol ligands can directly modulate transcription in plants.
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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.