ArticleMolecular and cellular biology2002
A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
- Glucose modulates IRF6 transcription factor dimerization to enable epidermal differentiation.Cell stem cell · 2025Article
- Mondo family proteins in diabetes.Frontiers in endocrinology · 2025Review
- Glucose-induced and ChREBP: MLX-mediated lipogenic program promotes hepatocellular carcinoma development.Oncogene · 2023Article
- The Function of MondoA and ChREBP Nutrient-Sensing Factors in Metabolic Disease.International journal of molecular sciences · 2023Review
- Multiomics Analysis Reveals Novel Genetic Determinants for Lens Differentiation, Structure, and Transparency.Biomolecules · 2023Review
- MEK1-dependent MondoA phosphorylation regulates glucose uptake in response to ketone bodies in colorectal cancer cells.Cancer science · 2023Article
- Review
- The Role of Mondo Family Transcription Factors in Nutrient-Sensing and Obesity.Frontiers in endocrinology · 2021Review
- The structure of importin α and the nuclear localization peptide of ChREBP, and small compound inhibitors of ChREBP-importin α interactions.The Biochemical journal · 2020Article
- Partitioning of MLX-Family Transcription Factors to Lipid Droplets Regulates Metabolic Gene Expression.Molecular cell · 2020Article
- Glucose-Sensing Transcription Factor MondoA/ChREBP as Targets for Type 2 Diabetes: Opportunities and Challenges.International journal of molecular sciences · 2019Review
- Glucose-6-Phosphate Upregulates Txnip Expression by Interacting With MondoA.Frontiers in molecular biosciences · 2019Article
- Validation, Identification, and Biological Consequences of the Site-specificMolecular & cellular proteomics : MCP · 2017Article
- Contrasting Patterns in the Evolution of Vertebrate MLX Interacting Protein (MLXIP) and MLX Interacting Protein-Like (MLXIPL) Genes.PloS one · 2016Article
- Functional interactions among members of the MAX and MLX transcriptional network during oncogenesis.Biochimica et biophysica acta · 2015Review
- MondoA-Mlx transcriptional activity is limited by mTOR-MondoA interaction.Molecular and cellular biology · 2015Article
- Coordination of nutrient availability and utilization by MAX- and MLX-centered transcription networks.Cold Spring Harbor perspectives in medicine · 2013Review
- Thioredoxin-interacting protein gene expression via MondoA is rapidly and transiently suppressed during inflammatory responses.PloS one · 2013Article
- Hormone-induced 14-3-3γ adaptor protein regulates steroidogenic acute regulatory protein activity and steroid biosynthesis in MA-10 Leydig cells.The Journal of biological chemistry · 2012Article
- Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
Among members of the bHLHZip family of transcriptional regulators, MondoA and Mlx have the unique property of cytoplasmic localization. We have proposed that MondoA-Mlx heterodimers accumulate in the nucleus in response to extracellular cues. Our previous work implicated heterodimerization between MondoA and Mlx and a conserved domain in the N terminus of MondoA as important determinants of MondoA-Mlx subcellular localization. MondoA and Mlx share sequence similarity in their bHLHZip domains and C termini. Here we show that for both MondoA and Mlx, this C-terminal domain has cytoplasmic localization activity that is required by the protein monomers to accumulate in the cytoplasm. This C-terminal domain is also a novel dimerization interface that functions independently of the leucine zipper to mediate heterotypic interactions between MondoA and Mlx. Dimerization between MondoA and Mlx inactivates the cytoplasmic localization activity of their C termini and is necessary for the heterocomplex to accumulate in the nucleus. MondoA-Mlx heterodimers, while poised for nuclear entry, are retained in the cytoplasm by conserved domains in the N terminus of MondoA. Mondo conserved regions (MCRs) II and III contribute to cytoplasmic localization of MondoA-Mlx by functioning as a CRM1-dependent nuclear export signal and as a novel binding site for 14-3-3 family members, respectively. We propose that the nuclear accumulation of MondoA and Mlx is a two-step process. First, heterodimerization abolishes the cytoplasmic localization activity of their C termini. Second, an extracellular signal(s) must overcome the cytoplasmic localization function imparted by CRM1 and 14-3-3 binding to the N terminus of MondoA.
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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.