ArticleThe Journal of cell biology2024
FER-like iron deficiency-induced transcription factor (FIT) accumulates in nuclear condensates.
Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Sulfur in dialogue with phosphorus, nitrogen, and iron: regulatory networks in plant nutrient homeostasis.Journal of experimental botany · 2026Review
- The CPK3-mediated cytosolic-nuclear translocation of bHLH107 recruits HY5 to regulate the CuJournal of advanced research · 2026Article
- Prediction of plant phase-separating proteins using positive-unlabeled learning.Genome biology · 2026Article
- Transcriptional outputs and condensates - formation and function.The New phytologist · 2026Review
- RNA polymerase II transcription compartments - from factories to condensates.Nature reviews. Genetics · 2025Review
- Decoding Long-Distance Communication Under Mineral Stress: Advances in Vascular Signalling and Molecular Tools for Plant Resilience.Plant, cell & environment · 2025Review
- Review
- Shedding light on iron nutrition: exploring intersections of transcription factor cascades in light and iron deficiency signaling.Journal of experimental botany · 2025Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The functional importance of nuclear protein condensation remains often unclear. The bHLH FER-like iron deficiency-induced transcription factor (FIT) controls iron acquisition and growth in plants. Previously described C-terminal serine residues allow FIT to interact and form active transcription factor complexes with subgroup Ib bHLH factors such as bHLH039. FIT has lower nuclear mobility than mutant FITmSS271AA. Here, we show that FIT undergoes a light-inducible subnuclear partitioning into FIT nuclear bodies (NBs). Using quantitative and qualitative microscopy-based approaches, we characterized FIT NBs as condensates that were reversible and likely formed by liquid-liquid phase separation. FIT accumulated preferentially in NBs versus nucleoplasm when engaged in protein complexes with itself and with bHLH039. FITmSS271AA, instead, localized to NBs with different dynamics. FIT colocalized with splicing and light signaling NB markers. The NB-inducing light conditions were linked with active FIT and elevated FIT target gene expression in roots. FIT condensation may affect nuclear mobility and be relevant for integrating environmental and Fe nutrition signals.
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Registered trials
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