Phospho-mutant activity assays provide evidence for alternative phospho-regulation pathways of the transcription factor FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR.
Amino Acid Sequence
Animals
Arabidopsis
/ metabolism
Arabidopsis Proteins
/ chemistry
Basic Helix-Loop-Helix Transcription Factors
/ chemistry
Biological Assay
/ methods
CHO Cells
Cricetinae
Cricetulus
Models, Biological
Mutation
/ genetics
Phosphorylation
Phosphotyrosine
/ metabolism
Protein Multimerization
Protein Stability
Transcriptional Activation
/ genetics
Arabidopsis
FIT
IRT1
bHLH039
iron uptake
serine phosphorylation
transcription factor
tyrosine phosphorylation
Journal
The New phytologist
ISSN: 1469-8137
Titre abrégé: New Phytol
Pays: England
ID NLM: 9882884
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
20
05
2019
accepted:
16
08
2019
pubmed:
6
9
2019
medline:
12
11
2020
entrez:
6
9
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 31487399
doi: 10.1111/nph.16168
pmc: PMC6916400
doi:
Substances chimiques
Arabidopsis Proteins
0
Basic Helix-Loop-Helix Transcription Factors
0
FIT1 protein, Arabidopsis
0
Phosphotyrosine
21820-51-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
250-267Informations de copyright
©2019 The Authors. New Phytologist ©2019 New Phytologist Trust.
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