ArticleMolecular and cellular biology2009
Metal-responsive transcription factor 1 (MTF-1) activity is regulated by a nonconventional nuclear localization signal and a metal-responsive transactivation domain.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- EP300-Mediated MTF1-K218 Lactylation Buffers AR-Driven Copper Overload to Suppress Cuproptosis in Castration-Resistant Prostate Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Combined metallomics and metabolomics reveal impact of metal homeostasis on biological pathways in C. elegans.Analytical and bioanalytical chemistry · 2026Article
- A New Toolbox to Label Zinc-MTF1 Responsive Neuronal Populations Unravels Cellular Congruence between MTF1 Responses and T-type Calcium Channelopathies in an Experimental Model of Epilepsy.Molecular neurobiology · 2025Article
- Navigating Transition Metal-Dependent Cell Death: Mechanisms, Crosstalk, and Future Directions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Emerging perspectives of copper-mediated transcriptional regulation in mammalian cell development.Metallomics : integrated biometal science · 2024Review
- Cellular zinc status alters chromatin accessibility and binding of p53 to DNA.Life science alliance · 2024Article
- Prognostic and Immunological Role of Cuproptosis-Related Gene MTF1 in Pan-Cancer.Journal of Cancer · 2024Article
- Cellular zinc status alters chromatin accessibility and binding of transcription factor p53 to genomic sites.bioRxiv : the preprint server for biology · 2023Article
- Genomic Redistribution of Metal-Response Transcription Factor-1 (MTF-1) in Cadmium Resistant Cells.Cells · 2023Article
- The Hippo pathway kinases LATS1 and LATS2 attenuate cellular responses to heavy metals through phosphorylating MTF1.Nature cell biology · 2022Article
- Integrated Analysis of Omics Data Reveal AP-1 as a Potential Regulation Hub in the Inflammation-Induced Hyperalgesia Rat Model.Frontiers in immunology · 2021Article
- Identification of novel activators of the metal responsive transcription factor (MTF-1) using a gene expression biomarker in a microarray compendium.Metallomics : integrated biometal science · 2020Article
- Zinc as a Therapeutic Agent in Bone Regeneration.Materials (Basel, Switzerland) · 2020Review
- The 9aaTAD Is Exclusive Activation Domain in Gal4.PloS one · 2017Article
- Short-lived mammals (shrew, mouse) have a less robust metal-responsive transcription factor than humans and bats.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2016Article
- The 9aaTAD Transactivation Domains: From Gal4 to p53.PloS one · 2016Article
- Cellular sensing and transport of metal ions: implications in micronutrient homeostasis.The Journal of nutritional biochemistry · 2015Review
- A Meloidogyne incognita effector is imported into the nucleus and exhibits transcriptional activation activity in planta.Molecular plant pathology · 2015Article
- Zinc supplementation protects against cadmium accumulation and cytotoxicity in Madin-Darby bovine kidney cells.PloS one · 2014Article
- Characterization of MtnE, the fifth metallothionein member in Drosophila.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metal-responsive transcription factor 1 (MTF-1) mediates both basal and heavy metal-induced transcription of metallothionein genes and also regulates other genes involved in the cell stress response and in metal homeostasis. In resting cells, MTF-1 localizes to both the cytoplasm and the nucleus but quantitatively accumulates in the nucleus upon metal load and under other stress conditions. Here we show that within the DNA-binding domain, a region spanning zinc fingers 1 to 3 (amino acids [aa] 137 to 228 in human MTF-1) harbors a nonconventional nuclear localization signal. This protein segment confers constitutive nuclear localization to a cytoplasmic marker protein. The deletion of the three zinc fingers impairs nuclear localization. The export of MTF-1 to the cytoplasm is controlled by a classical nuclear export signal (NES) embedded in the acidic activation domain. We show that this activation domain confers metal inducibility in distinct cell types when fused to a heterologous DNA-binding domain. Furthermore, the cause of a previously described stronger inducibility of human versus mouse MTF-1 could be narrowed down to a 3-aa difference in the NES; "humanizing" mouse MTF-1 at these three positions enhanced its metal inducibility to the level of human MTF-1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.