A cryptic START domain regulates deeply conserved transcription factors

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ID: 327937
2026
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Abstract
Transcription factors (TFs) integrate a diverse array of inputs to achieve the exquisite control of gene expression necessary for life. In plants, this is exemplified by the deeply conserved CLASS III HOMEODOMAIN LEUCINE ZIPPER (HD-ZIPIII) family of TFs. HD-ZIPIII activity is controlled by inputs at transcriptional, post-transcriptional, and post-translational levels. As part of their multidomain architecture, HD-ZIPIII TFs contain a StAR-related lipid transfer (START) domain, a ubiquitously distributed evolutionary module that binds various types of lipophilic ligands. Here, we show that HD-ZIPIII and HD-ZIPIV proteins contain a cryptic, deeply conserved START domain which we term the disorder-containing START domain (dSTART). The dSTART domain is required for HD-ZIPIII developmental function, controlling their subcellular localization and DNA-binding properties. The dSTART domain also helps discriminate responsive from non-responsive binding sites across the HD-ZIPIII shared genetic network. Finally, we identify candidate ligands of the dSTART domain including several species of phosphatidylglycerol and phosphatidic acid. The identification and functional characterization of a cryptic START domain provides new mechanistic insights into a deeply conserved family of TFs with roles in nearly all aspects of plant development.
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Authors Courtney E. Dresden, Ekaterina P. Andrianova, Brian J. Smith, Nicole I. Callery, Dominic Kolonay, Ashton S. Holub, Ricardo A. Urquidi Camacho, Sarah G. Choudury, I. J. Higgins, Igor B. Zhulin, Aman Y. Husbands
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Journal The Plant cell
Year 2026
DOI
10.1093/plcell/koag267
URL
https://doi.org/10.1093/plcell/koag267
Keywords Keywords not found

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