ArticleThe New phytologist2020
Phospho-mutant activity assays provide evidence for alternative phospho-regulation pathways of the transcription factor FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR.
Article in The New phytologist, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 33 citations in OpenAlex.
- CITF1 interacts with FIT and regulates copper-iron crosstalk in Arabidopsis.The Plant cell · 2026Article
- Regulation of vacuole fusion in stomata by dephosphorylation of the HOPS subunit VPS39.The Plant journal : for cell and molecular biology · 2025Article
- Abscisic acid regulates iron accumulation in plant seeds via the PYLs-bHLH IVc-YSLs module.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The transcription factor MYB30 promotes iron homeostasis by maintaining the stability of the FIT transcription factor.The Plant cell · 2025Article
- Calmodulin-like protein MdCML15 interacts with MdBT2 to modulate iron homeostasis in apple.Horticulture research · 2024Article
- FER-like iron deficiency-induced transcription factor (FIT) accumulates in nuclear condensates.The Journal of cell biology · 2024Article
- The small iron-deficiency-induced protein OLIVIA and its relation to the bHLH transcription factor POPEYE.PloS one · 2024Article
- SEC14-GOLD protein PATELLIN2 binds IRON-REGULATED TRANSPORTER1 linking root iron uptake to vitamin E.Plant physiology · 2023Article
- Iron uptake, signaling, and sensing in plants.Plant communications · 2022Review
- The Iron Deficiency-Regulated Small Protein Effector FEP3/IRON MAN1 Modulates Interaction of BRUTUS-LIKE1 With bHLH Subgroup IVc and POPEYE Transcription Factors.Frontiers in plant science · 2022Article
- Autophagy Mediates the Degradation of Plant ESCRT Component FREE1 in Response to Iron Deficiency.International journal of molecular sciences · 2021Article
- All together now: regulation of the iron deficiency response.Journal of experimental botany · 2021Review
- Regulatory Mechanisms of bHLH Transcription Factors in Plant Adaptive Responses to Various Abiotic Stresses.Frontiers in plant science · 2021Review
- Comparative Physiological and Transcriptomic Analyses Reveal Altered Fe-Deficiency Responses in Tomato EpimutantFrontiers in plant science · 2021Article
- Further insights into the role of bHLH121 in the regulation of iron homeostasis inPlant signaling & behavior · 2020Article
- FIT, a regulatory hub for iron deficiency and stress signaling in roots, and FIT-dependent and -independent gene signatures.Journal of experimental botany · 2020Review
- Mobility and localization of the iron deficiency-induced transcription factor bHLH039 change in the presence of FIT.Plant direct · 2019Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The key basic helix-loop-helix (bHLH) transcription factor in iron (Fe) uptake, FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR (FIT), is controlled by multiple signaling pathways, important to adjust Fe acquisition to growth and environmental constraints. FIT protein exists in active and inactive protein pools, and phosphorylation of serine Ser272 in the C-terminus, a regulatory domain of FIT, provides a trigger for FIT activation. Here, we use phospho-mutant activity assays and study phospho-mimicking and phospho-dead mutations of three additional predicted phosphorylation sites, namely at Ser221 and at tyrosines Tyr238 and Tyr278, besides Ser 272. Phospho-mutations at these sites affect FIT activities in yeast, plant, and mammalian cells. The diverse array of cellular phenotypes is seen at the level of cellular localization, nuclear mobility, homodimerization, and dimerization with the FIT-activating partner bHLH039, promoter transactivation, and protein stability. Phospho-mimicking Tyr mutations of FIT disturb fit mutant plant complementation. Taken together, we provide evidence that FIT is activated through Ser and deactivated through Tyr site phosphorylation. We therefore propose that FIT activity is regulated by alternative phosphorylation pathways.
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