Molecular insights into dimerization inhibition of c-Maf transcription factor

Pellegrino, Sara; Ronda, Luca; Annoni, Chiara; Contini, Alessandro; Erba, Emanuela; Gelmi, Maria Luisa; Piano, Riccardo; Paredi, Gianluca; Mozzarelli, Andrea; Bettati, Stefano

doi:10.1016/j.bbapap.2014.09.003

Cited by 15 publications

(13 citation statements)

References 45 publications

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“…The conformational behaviour of peptides and their complexes were investigated in water by CD experiments (Figure 1). CD is indeed a powerful tool to detect conformational changes also in short peptides 41,46 . As expected, the CD spectra of His7 and Mets7 alone were characterized by the presence of a negative band at around 195–198 nm, indicating the absence of a preferred conformation.…”

Section: Resultssupporting

confidence: 66%

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Exploring the copper binding ability of Mets7 hCtr‐1 protein domain and His7 derivative: An insight in Michael addition catalysis

Rimoldi

Bucci

Feni

et al. 2020

Journal of Peptide Science

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Mets7 is a methionine-rich motif present in hCtr-1 transporter that is involved in copper cellular trafficking. Its ability to bind Cu(I) was recently exploited to develop metallopeptide catalysts for Henry condensation. Here, the catalytic activity of Mets7-Cu(I) complex in Michael addition reactions has been evaluated. Furthermore, His7 peptide, in which Met residues have been substituted with His ones, was also prepared. This substitution allowed His7 to coordinate Cu(II), with the obtainment of a stable turn conformation as evicted by CD experiments. His7-Cu(II) proved also to be a better catalyst than Mets7-Cu(I) in the addition reaction. In particular, when the substrate was the (E)-1-phenyl-3-(pyridin-2-yl)prop-2-en-1one, a conversion of 71% and a significative 58 % of e.e. was observed.

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Section: Resultssupporting

confidence: 66%

“…CD is indeed a powerful tool to detect conformational changes also in short peptides. 41,46 As expected, the CD spectra of His7 and Mets7 alone were characterized by the presence of a negative band at around Conversion and enantiomeric excess were determined by HPLC (see Table T2 in the Supporting Information).…”

Section: Resultsmentioning

confidence: 57%

Exploring the copper binding ability of Mets7 hCtr‐1 protein domain and His7 derivative: An insight in Michael addition catalysis

Rimoldi

Bucci

Feni

et al. 2020

Journal of Peptide Science

Self Cite

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“…Transcriptional regulation by the MafA and MafB proteins is achieved by homo-or heterodimer binding to large Maf-response elements (32)(33)(34). ChIP analysis demonstrated MafB-induced binding to MafA-regulated Insulin and G6pc2 gene transcriptional control sequences in bMafBTg nuclei (Fig.…”

Section: Development Of a B-cell-specific Mafb Overexpression Mouse Mmentioning

confidence: 95%

Examining How the MAFB Transcription Factor Affects Islet β-Cell Function Postnatally

et al. 2018

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The sustained expression of the MAFB transcription factor in human islet β-cells represents a distinct difference in mice. Moreover, mRNA expression of closely related and islet β-cell–enriched MAFA does not peak in humans until after 9 years of age. We show that the MAFA protein also is weakly produced within the juvenile human islet β-cell population and that MafB expression is postnatally restricted in mouse β-cells by de novo DNA methylation. To gain insight into how MAFB affects human β-cells, we developed a mouse model to ectopically express MafB in adult mouse β-cells using MafA transcriptional control sequences. Coexpression of MafB with MafA had no overt impact on mouse β-cells, suggesting that the human adult β-cell MAFA/MAFB heterodimer is functionally equivalent to the mouse MafA homodimer. However, MafB alone was unable to rescue the islet β-cell defects in a mouse mutant lacking MafA in β-cells. Of note, transgenic production of MafB in β-cells elevated tryptophan hydroxylase 1 mRNA production during pregnancy, which drives the serotonin biosynthesis critical for adaptive maternal β-cell responses. Together, these studies provide novel insight into the role of MAFB in human islet β-cells.

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“…Another possible way to inhibit c-Maf activity is by preventing its dimerization. This could be achieved by the design of specific peptide able to destabilize homodimers of c-Maf (126). An older study described that glucocorticoids are potential inhibitors of c-Maf in multiple myeloma (127).…”

Section: Perspectives: Manipulating C-maf Expression To Treat Patients?mentioning

confidence: 99%

c-MAF, a Swiss Army Knife for Tolerance in Lymphocytes

et al. 2020

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Beyond its well-admitted role in development and organogenesis, it is now clear that the transcription factor c-Maf has owned its place in the realm of immune-related transcription factors. Formerly introduced solely as a Th2 transcription factor, the role attributed to c-Maf has gradually broadened over the years and has extended to most, if not all, known immune cell types. The influence of c-Maf is particularly prominent among T cell subsets, where c-Maf regulates the differentiation as well as the function of multiple subsets of CD4 and CD8 T cells, lending it a crucial position in adaptive immunity and anti-tumoral responsiveness. Recent research has also revealed the role of c-Maf in controlling Th17 responses in the intestine, positioning it as an essential factor in intestinal homeostasis. This review aims to present and discuss the recent advances highlighting the particular role played by c-Maf in T lymphocyte differentiation, function, and homeostasis.

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Molecular insights into dimerization inhibition of c-Maf transcription factor

Cited by 15 publications

References 45 publications

Exploring the copper binding ability of Mets7 hCtr‐1 protein domain and His7 derivative: An insight in Michael addition catalysis

Exploring the copper binding ability of Mets7 hCtr‐1 protein domain and His7 derivative: An insight in Michael addition catalysis

Examining How the MAFB Transcription Factor Affects Islet β-Cell Function Postnatally

c-MAF, a Swiss Army Knife for Tolerance in Lymphocytes

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