| 1993 |
MafF is a nuclear bZIP protein that lacks a transcriptional activation domain (N-terminal acidic domain), localizes to the nucleus, and does not induce morphological transformation of chicken embryo fibroblasts but can weakly induce colony formation in soft agar when overexpressed via retroviral vector. |
Structural analysis, retroviral overexpression, immunofluorescence, soft agar colony assay |
Oncogene |
Medium |
8361754
|
| 1999 |
Human MafF (hMafF) binds specifically to the US-2 DNA element in the oxytocin receptor (OTR) gene promoter, as demonstrated by electrophoretic mobility shift assay, and its protein is preferentially expressed in term myometrium, supporting a role in OTR gene upregulation at parturition. |
Yeast one-hybrid screen, EMSA, Northern/Western blot |
Biochemical and biophysical research communications |
Medium |
10527846
|
| 1999 |
MafF is dispensable for normal development in mice: homozygous mafF null mutant mice are born in normal Mendelian ratios with no obvious functional deficiencies, and lacZ knock-in reveals prominent expression in gut, lung, liver, outflow tract of heart, cartilage, bone membrane, and skin but not in hematopoietic cells. |
Gene targeting (knockout), lacZ reporter knock-in, developmental expression analysis |
The Journal of biological chemistry |
High |
10409670
|
| 2002 |
MafF can form homodimers and high-affinity heterodimers with CNC-bZIP family members Nrf1, Nrf2, and NF-E2; MafF homodimers do not repress transcription on gamma-globin, beta-globin, or GCS1 promoters in multiple cell lines, whereas MafF/CNC heterodimers act as weak transcriptional activators; in combination with Jun on the GCS1 promoter, MafF shows a specific regulatory role. |
Co-immunoprecipitation, promoter-reporter assays, overexpression in multiple cell lines |
Blood cells, molecules & diseases |
Medium |
12490281
|
| 2002 |
mafF mRNA expression is induced to the greatest extent among the three small Maf genes by electrophile response element (EpRE) activators PDTC and PEITC (but not tBHQ) in HepG2 cells, and this induction is transcriptionally mediated, indicating mafF is a stress-responsive gene regulated via mechanisms distinct from mafG and mafK. |
Northern/RT-PCR, actinomycin D transcription block, multiple cell lines |
The Biochemical journal |
Medium |
11772409
|
| 2005 |
MAFF transcript and protein levels are rapidly induced (within 30 min) by proinflammatory cytokines IL-1β and TNF in PHM1-31 myometrial cells at the transcriptional level (blocked by actinomycin D); this induction is specific to MAFF and not shared by MAFG or MAFK. |
RT-PCR, Western blot with MAFF-specific antiserum, actinomycin D block, time-course experiments |
Biology of reproduction |
Medium |
16371591
|
| 2006 |
A novel protein MIP (MafF interacting protein) interacts with hMafF via its coiled-coil domain binding to the leucine zipper of hMafF; this interaction causes MIP to translocate from the cytoplasm to the nucleolus; co-expression of MIP and hMafF (but not either alone) activates transcription from a promoter containing US2 elements. |
In vitro pull-down, co-immunoprecipitation, subcellular localization by fluorescence microscopy, promoter-reporter assay, domain truncation |
Archives of biochemistry and biophysics |
Medium |
16549056
|
| 2016 |
Small Maf proteins including MafF form homodimers (acting as transcriptional repressors lacking activation domain) and heterodimers with CNC proteins (p45 NF-E2, Nrf1, Nrf2, Nrf3) and Bach proteins (Bach1, Bach2); CNC and Bach proteins cannot bind DNA as monomers and require sMaf as obligatory partners; heterodimer function (activation or repression) depends on the partner. |
Review integrating prior biochemical, genetic, and structural data from multiple labs |
Gene |
High |
27058431
|
| 2019 |
MAFF directly binds to the CXCL1 and CSF3 gene promoters and is required for their transcriptional activation in myometrial cells; MAFF knockdown significantly reduces CXCL1 and CSF3 transcript and protein levels, and MAFF-dependent signaling in myometrial cells can regulate cytokine and matrix metalloproteinase expression in THP-1 monocytic cells in a paracrine fashion. |
siRNA knockdown, chromatin immunoprecipitation (ChIP), RT-qPCR, protein measurements, paracrine co-culture assay |
Journal of cellular and molecular medicine |
Medium |
30669188
|
| 2021 |
MAFF forms a heterodimer with BACH1 that directly targets and transcriptionally activates the IL11 gene promoter in hypoxic breast cancer cells; IL11 activation leads to downstream STAT3 signaling to promote tumor invasion and metastasis; MAFF expression is induced by HIF under hypoxia. |
ChIP-seq, RNA-seq, siRNA knockdown, overexpression, invasion assays, in vivo metastasis models, IL11 inhibition |
Nature communications |
High |
34262028
|
| 2021 |
MAFF transcription is activated by a circRNA (cia-MAF) that binds to the MAFF promoter and recruits the TIP60 histone acetyltransferase complex; loss of cia-MAF reduces TIP60 complex binding at the MAFF promoter and decreases MAFF expression, impacting liver tumor-initiating cell self-renewal and metastasis. |
circRNA knockout (CRISPR), promoter binding assays, ChIP for TIP60 complex, overexpression, xenograft models |
The Journal of clinical investigation |
Medium |
34403373
|
| 2021 |
In hepatocellular carcinoma, MafF is a direct target of miR-224-5p; circular RNA circ-ITCH sponges miR-224-5p to stabilize MafF expression; MafF overexpression inhibits HCC cell proliferation and induces apoptosis, acting as a tumor suppressor. |
Luciferase reporter assay, RNA pull-down assay, lentiviral overexpression, rescue experiments, proliferation and apoptosis assays |
Oncology research |
Medium |
31969212
|
| 2021 |
MafF suppresses transcription from the HBV core promoter by physically binding to the promoter and competitively inhibiting HNF-4α binding to an overlapping sequence in enhancer II (EnhII); MafF expression is induced by IL-1β or TNF-α in an NF-κB-dependent manner. |
siRNA knockdown, CRISPR/Cas9 knockout, ChIP, overexpression with mutant binding site, HBV reporter virus, NF-κB inhibition |
Journal of virology |
High |
33980595
|
| 2021 |
MAFF positively correlates with LDLR expression in non-inflammatory conditions but, upon LPS stimulation, forms heterodimers with BACH1 that bind the MAF recognition element (MARE) in the LDLR promoter to transcriptionally downregulate LDLR expression; BACH1 is identified as MAFF's partner under inflammatory conditions by ChIP-mass spectrometry. |
ChIP-seq, ChIP-mass spectrometry (ChIP-MS), siRNA knockdown, overexpression, in vivo mouse experiments, human patient correlation |
Circulation |
High |
33626882
|
| 2021 |
miR-320a directly targets MafF mRNA (validated by RIP-Seq and luciferase reporter assay); overexpression of miR-320a inhibits MafF protein expression, increases ROS, inhibits β-cell proliferation, and induces apoptosis, causing pancreatic β-cell dysfunction. |
RIP-Seq, luciferase reporter assay, Western blotting, AAV8-mediated β-cell specific overexpression/inhibition, islet transplantation, hyperglycemic clamp |
Molecular therapy. Nucleic acids |
Medium |
34631276
|
| 2024 |
BAP1, a nuclear deubiquitinating enzyme, binds to MAFF and removes K48-linked ubiquitin chains, stabilizing MAFF protein; stabilized MAFF upregulates DUSP5 expression, resulting in inhibition of ERK phosphorylation and suppression of colorectal cancer growth. |
Quantitative proteomics, Co-IP, DUB library screen, ubiquitination assays (K48-specific), MAFF overexpression/knockdown, in vitro and xenograft models, RNA-seq |
European journal of cancer |
High |
39151323
|
| 2024 |
MAFF directly binds to the ZNF711 promoter and represses its transcription; MAFF also interacts with BATF3 (demonstrated by co-immunoprecipitation and co-localization), and BATF3 similarly binds the ZNF711 promoter; simultaneous knockdown of BATF3 and MAFF phenocopies single knockdowns on ZNF711 transcription and apoptosis, indicating MAFF-BATF3 heterodimer represses ZNF711. |
Dual luciferase assay, ChIP-PCR, Co-IP, immunofluorescence, knockdown rescue experiments |
Chemico-biological interactions |
Medium |
38908812
|
| 2024 |
MAFF regulates ferroptosis and cell cycle progression in lung adenocarcinoma by directly controlling transcription of SLC7A11, CDK6, and CDKN2C (identified by ChIP-seq and RNA-seq); MAFF loss promotes cell cycle G1-to-S progression and reduces ferroptosis sensitivity; the cAMP/PKA/CREB1 intracellular pathway upregulates MAFF expression in response to cisplatin or ionizing radiation. |
CRISPR screens, ChIP-seq, RNA-seq, single-cell RNA-seq, xenograft models, pharmacological cAMP/PKA pathway analysis |
Drug resistance updates |
High |
38266355
|
| 2025 |
MAFF and BACH1 form a heterodimer that directly binds to the CLCF1 gene promoter (identified by CUT&Tag and RNA-seq) to transcriptionally activate CLCF1, which subsequently activates STAT3 signaling to protect against hepatic ischemia-reperfusion injury by reducing apoptosis and inflammation. |
CUT&Tag, RNA-seq, adenovirus-mediated overexpression, mouse I/R model |
Cellular & molecular biology letters |
Medium |
40169936
|
| 2025 |
YTHDC1 (an m6A reader) promotes nuclear export and stability of MAFF mRNA, enhancing MAFF translation; MAFF in turn transcriptionally activates VMP1, protecting hepatocytes from oxidative stress in ischemia/reperfusion injury. |
Knockdown/overexpression of YTHDC1 and MAFF, VMP1 rescue experiments, mouse I/R model, mechanistic mRNA stability/export assays |
Cellular signalling |
Medium |
40054588
|
| 2025 |
ZNF655 promotes nuclear translocation of MAFF in ovarian cancer cells; nuclear MAFF directly binds the CCND1 promoter and activates its transcription, driving proliferation and stemness; MAFF knockdown phenocopies ZNF655 depletion. |
Co-IP, ChIP, reporter assay, knockdown/overexpression, xenograft models |
Cancer cell international |
Medium |
41088232
|
| 2025 |
MAFF suppresses nuclear translocation of YAP1 in non-small cell lung cancer cells, reducing downstream VEGF and CTGF expression and inhibiting angiogenesis; MAFF overexpression reduces tumor growth and microvessel density in vivo. |
Western blot, immunofluorescence, overexpression, xenograft models, IHC for microvessel density |
PeerJ |
Medium |
41287850
|
| 2025 |
HDAC6 deacetylates MAFF to suppress its expression; loss of MAFF derepresses KLF5 transcription (MAFF directly suppresses KLF5 promoter activity as shown by ChIP and dual luciferase reporter assay), thereby enhancing renal fibrosis and inflammation in lupus nephritis. |
ChIP, dual luciferase reporter assay, HDAC6 inhibition, overexpression/knockdown, in vitro and MRL/lpr mouse model |
Renal failure |
Medium |
39412062
|
| 2025 |
NRF2 and MAFF directly target the promoters of contraction-associated protein genes PTGS2 and OXTR (confirmed by dual-luciferase reporter assay) downstream of melatonin-MT2 receptor-PKC signaling; silencing NRF2 or MAFF reduces contraction-associated protein expression and attenuates myometrial contractility. |
Dual-luciferase reporter assay, siRNA knockdown, collagen gel contraction assay, pharmacological receptor and kinase inhibition |
Journal of pineal research |
Medium |
41854048
|
| 2025 |
MAFF directly binds the AKR1C1 promoter (confirmed by dual-luciferase reporter assay) and transcriptionally activates AKR1C1; the MAFF-AKR1C1 axis inhibits ferroptosis by reducing MDA accumulation and lipid ROS, thereby promoting pancreatic cancer progression. |
Dual-luciferase reporter assay, MAFF knockdown in cell lines, xenograft models, transcriptome sequencing |
QJM : monthly journal of the Association of Physicians |
Medium |
41206944
|