ArticleThe Plant cell2026
A cryptic START domain regulates deeply conserved transcription factors.
Article in The Plant cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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-Zip III) family of TFs. HD-Zip III activity is controlled by inputs at transcriptional, post-transcriptional, and post-translational levels. As part of their multidomain architecture, HD-Zip III 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-Zip III and HD-Zip IV proteins contain an additional cryptic, deeply conserved START domain which we term the disorder-containing START domain (dSTART). The dSTART domain is required for HD-Zip III developmental function, promoting homodimerization and controlling subcellular localization and DNA-binding competence. The dSTART domain also helps discriminate responsive from nonresponsive binding sites across the HD-Zip III shared genetic network. Finally, we identify candidate ligands of the dSTART domain including several species of phosphatidylglycerol. 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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