Alternative titles; symbols
HGNC Approved Gene Symbol: MAF
Cytogenetic location: 16q23.2 Genomic coordinates (GRCh38): 16:79,202,622-79,600,737 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 16q23.2 | Ayme-Gripp syndrome | 601088 | Autosomal dominant | 3 |
| Cataract 21, multiple types | 610202 | Autosomal dominant | 3 |
MAF encodes a transcription factor involved in T-helper-2 (Th2) cell differentiation. MAF is also required for efficient development of Th17 cells, and it controls transcription of the gene encoding interleukin-4 (IL4; 147780) in CD4 (186940)-positive follicular helper T cells (summary by Ranzani et al., 2015).
Nishizawa et al. (1989) identified in the human genome a cellular analog of v-maf which was isolated from the provirus of the avian musculoaponeurotic fibrosarcoma virus AS42. The deduced amino acid sequence of the v-maf gene product contains a leucine zipper motif similar to that found in a number of DNA-binding proteins, including the gene products of the FOS (164810), JUN (165160), and MYC (190080) oncogenes.
Ring et al. (2000) cloned mouse Maf, which encodes a deduced 370-amino acid protein. In situ hybridization and X-gal staining of mouse embryos revealed widespread Maf expression, including in perichondrium of axial and appendicular skeleton, forebrain, kidney, and developing eye. Maf expression was first detected in eye between embryonic days 10.5 and 11, when posterior cells of the lens vesicle begin to differentiate into elongated primary lens fiber cells.
By screening for genes expressed in mouse nervous system, Wende et al. (2012) found that Maf was expressed in neurons of rapidly-adapting mechanoreceptors of the lumbar dorsal root ganglia (DRG). Maf expression started around embryonic day 11. Immunohistochemical analysis revealed similar MAF expression in human DRG.
Niceta et al. (2015) performed immunohistochemical analysis of mouse embryos and confirmed previously reported widespread Maf staining in the lens, dorsal spinal cord, dorsal root ganglia, skin, kidney, hypertrophic chondrocytes of vertebrae, rib and limb cartilage, and the cartilage primordium of the basioccipital bone. Niceta et al. (2015) detected a specific and strong signal in cochlear cells of E14.5 embryos.
Through the use of a cDNA probe for in situ hybridization, Yoshida et al. (1991) localized the MAF gene to chromosome 16q22-q23. Jamieson et al. (2002) reported that the MAF gene maps to chromosome 16q23.2.
Blank and Andrews (1997) reviewed the MAF transcription factors, a unique subclass of basic-leucine zipper transcription (bZIP) factors. Members of the MAF family appear to play important roles in the regulation of differentiation.
Minimal change nephrotic syndrome (MCNS), also known as lipoid nephrosis, is a glomerular disease characterized by heavy proteinuria that remits with abatement of cell-mediated immunity. Shalhoub (1974) postulated that MCNS results from abnormal T-cell activation. By subtractive cloning and differential screening analyses using MCNS patient T lymphocytes, Sahali et al. (2002) identified a number of genes differentially regulated in MCNS. The findings suggested that MCNS relapse might be associated with a Th2 response, in part due to downregulation of IL12RB2 (601642), a Th1-associated cytokine receptor, and selective recruitment of MAF, which promotes Th2 responses.
Aziz et al. (2009) reported that combined deficiency for the transcription factors MafB and c-Maf enables extended expansion of mature monocytes and macrophages in culture without loss of differentiated phenotype and function. Upon transplantation, the expanded cells are nontumorigenic and contribute to functional macrophage populations in vivo. Small hairpin RNA inactivation showed that continuous proliferation of MafB/c-Maf-deficient macrophages requires concomitant upregulation of 2 pluripotent stem cell-inducing factors, KLF4 (602253) and c-Myc. Aziz et al. (2009) concluded that MafB/c-Maf deficiency renders self-renewal compatible with terminal differentiation. It thus appears possible to amplify functional differentiated cells without malignant transformation or stem cell intermediates.
Sato et al. (2011) reported that Maf was highly expressed in mouse Th2 and Th17 cells, whereas Gata3 (131320) was only expressed in Th2 cells. Luciferase analysis showed that Maf induced Il23r (607562) promoter activity, likely via binding to a MAF recognition element (MARE) within the promoter. Sato et al. (2011) concluded that MAF is a versatile transcription factor that is involved in the development and/or maintenance of memory Th cells, particularly Th17 cells.
MFTRR (616264) is a chromatin-associated long intergenic noncoding RNA (lincRNA) specific to CD4-positive Th1 cells. Ranzani et al. (2015) found that expression of the neighboring genes MAF and MFTRR was inversely correlated, with Th1 cells showing high expression of MFTRR and low expression of MAF, and Th2 and Th17 cells showing low expression of MFTRR and high expression of MAF. Knockdown of MAFTRR via small interfering RNA in activated CD4-positive naive T cells led to increased MAF expression. Th2 cells showed increased RNA polymerase II binding and increased abundance of histone trimethylated at lys4 in the MAF promoter region compared with Th1 cells. RNA immunoprecipitation analysis detected interaction of MFTRR with the chromatin modifiers EZH2 (601573) and LSD1 (KDM1A; 609132). Knockdown of MFTRR was associated with reduced abundance of EZH2 and LSD1 and decreased EZH2 enzyme activity at the MAF promoter. Ranzani et al. (2015) concluded that there is a long-distance interaction between the genomic regions of MFTRR and MAF, with MFTRR acting as a scaffold to recruit EZH2 and LSD1 and to modulate EZH2 enzyme activity at the MAF promoter, thus regulating MAF transcription.
Using RNA and protein expression profiling at single-cell resolution in mouse cells, Chihara et al. (2018) identified a module of coinhibitory receptors that includes not only several known coinhibitory receptors but many novel surface receptors. Chihara et al. (2018) functionally validated 2 novel coinhibitory receptors, activated protein C receptor (PROCR; 600646) and podoplanin (PDPN; 608863). The module of coinhibitory receptors is coexpressed in both CD4+ and CD8+ T cells and is part of a larger coinhibitory gene program that is shared by nonresponsive T cells in several physiologic contexts and is driven by the immunoregulatory cytokine IL27 (608273). Computational analysis identified the transcription factors PRDM1 (603423) and c-MAF as cooperative regulators of the coinhibitory module, and this was validated experimentally. This molecular circuit underlies the coexpression of coinhibitory receptors in T cells and identifies regulators of T cell function with the potential to control autoimmunity and tumor immunity.
Jamieson et al. (2002) identified a family where ocular developmental abnormalities cosegregated with a translocation, t(5;16)(p15.3;q23.2), in both balanced and unbalanced forms. Cloning the 16q23.2 breakpoint demonstrated that it transected the genomic-control domain of MAF. The 16q23.2 breakpoint also transected the common fragile site FRA16D (see 605131), providing a molecular demonstration of a germline break in a common fragile site.
Cataract 21, Multiple Types
Through mutation screening of a panel of patients with hereditary congenital cataract, Jamieson et al. (2002) identified a mutation in the MAF gene (177075.0001) in a 3-generation family with autosomal dominant juvenile-onset pulverulent cataract (CTRCT21; 610202).
In a 3-generation family with cerulean congenital cataract, Vanita et al. (2006) sequenced the MAF gene and identified a heterozygous missense mutation in the MAF gene (177075.0002) that cosegregated with the disease. The mutation was not found in 106 unrelated controls.
In 3 families and 1 sporadic patient with cataract and microcornea, Hansen et al. (2007) analyzed 13 lens-expressed cataract genes and identified heterozygosity for a missense mutation in the MAF gene (R299S; 177075.0003) in 1 family. Hansen et al. (2007) noted that all 3 of the reported cataract-associated MAF mutations are located in the basic region of the DNA-binding domain in alpha-helix-3, suggestive of a mutational hotspot.
In affected members of a 3-generation Japanese family who had congenital cataract with or without microcornea, Narumi et al. (2014) performed whole-exome sequencing and identified a heterozygous missense mutation in the MAF gene (Q303P; 177075.0004).
Ayme-Gripp Syndrome
In 8 unrelated patients with congenital cataract, deafness, intellectual disability, seizures, and a Down syndrome-like facies (Ayme-Gripp syndrome; 601088), Niceta et al. (2015) identified heterozygosity for de novo missense mutations in the MAF gene (see, e.g., 177075.0005-177075.0010). Functional analyses demonstrated that all Ayme-Gripp-associated mutants accumulated in cells as unphosphorylated proteins, in sharp contrast to cells expressing wildtype MAF or the cataract-associated R288P mutant (177075.0001), in which the phosphorylated protein dominated and unphosphorylated MAF was barely detectable. In a zebrafish model, Niceta et al. (2015) used measurement of the optic tectum as a surrogate for brain volume, reduction in which correlates with neurodevelopmental defects in humans. They found that Ayme-Gripp-associated mutations caused a statistically significant reduction in the size of the optic tectum, compared to wildtype MAF or the R288P mutant, which did not induce appreciable brain volume differences.
By generating healthy mice overexpressing mouse Maf in immature and mature T cells, Ho et al. (1998) confirmed that Maf transactivates expression of Il4. Levels of serum IgE and IgG1, but not Ifng (147570)-dependent IgG2a, were higher in transgenic mice than in their wildtype littermates. Splenocytes derived from Maf-transgenic mice, in a gene dose-dependent manner, differentiated into Th2 cells, whereas wildtype splenocytes under the same conditions became Th1 cells. Splenocytes from Maf-transgenic mice lacking Il4 failed to undergo Th2 differentiation, but they could differentiate into Th1 cells. Maf overexpression alone was insufficient to induce Il4 production by normal Th1 cells. Ho et al. (1998) concluded that overexpression of MAF skews the Th response to a Th2 type via IL4-dependent and -independent mechanisms.
Kim et al. (1999) demonstrated that the homozygous null mutant Maf mouse embryo exhibits defective lens formation and microphthalmia.
Ring et al. (2000) found that Maf -/- mouse embryos exhibited a slightly foreshortened head and abnormal lens development, and that nearly all died within a few hours of birth. The 1 surviving animal exhibited microphthalmia, followed by cutaneous closure of the ocular chamber. Fiber cell differentiation and elongation ceased by embryonic day 12.5 in Maf -/- lens, with persistence of a hollow lens vesicle and absence of alpha-crystallin (see CRYAA; 123580) expression. Cells at the equatorial zone of the lens withdrew from the cell cycle and began to express fiber cell-specific proteins, but they failed to elongate and differentiate normally. After embryonic day 16.5, the mutant vesicle became progressively deformed. Ring et al. (2000) identified functional MAF-binding sites in the promoter regions of mouse alpha-A-crystallin (CRYAA), mouse beta-B2 crystallin (CRYBB2; 123620), and human beta-A4-crystallin (CRYBA4; 123631). They concluded that Maf deficiency causes a profound defect in early maturation of primary and secondary lens fiber cells.
Lyon et al. (2003) reported a mouse mutant which in the heterozygous state exhibits mild pulverulent cataract named 'opaque flecks in lens' (Ofl). The mutant was shown to be allelic with a knockout of Maf. Homozygotes for Ofl and for Maf null mutations were similar except for the addition of renal tubular nephritis in surviving Ofl homozygotes. Sequencing identified the mutation as a 1803G-A transition, leading to an arg291-to-gln (R291Q) substitution in the basic region of the DNA-binding domain. Since mice heterozygous for Maf knockouts showed no cataracts, the authors suggested that the Ofl R291Q mutant protein may have a dominant effect. The mutation also resulted in a selective alteration in DNA binding affinities to target oligonucleotides containing variations in core CRE and TRE elements. The authors hypothesized that arginine-291 may be important for core element binding and suggested that the mutant protein may exert a differential downstream effect among its binding targets.
By ethylnitrosourea (ENU) mutagenesis, Perveen et al. (2007) identified a semidominant mouse c-Maf mutation, resulting in a asp90-to-val (D90V) substitution at a highly conserved residue within the N-terminal minimal transactivation domain (MTD). The phenotype of D90V homozygotes was isolated cataract. Functional analysis revealed that the D90V mutation results in increased promoter activation and enhances p300 (602700) recruitment in a cell type-dependent manner. Perveen et al. (2007) observed similar enhancement of p300 interaction with the S50T mutation in the MTD of the NRL gene (162080.0001), which suggests a common mechanism of action.
Wende et al. (2012) found that conditional knockout of Maf in mouse DRG cells disrupted the architecture and function of several rapidly adapting mechanoreceptor subtypes. Pacinian corpuscles, specialized to detect high-frequency vibrations, were severely atrophied, with loss of innervating axons. In vitro skin-saphenous nerve preparations of Maf-knockout mice revealed abnormal fire response to mechanical stimuli.
In 5 affected members of a 3-generation family with autosomal dominant juvenile-onset cataract (CTRCT21; 610202), Jamieson et al. (2002) identified a 1670G-C transversion in the MAF gene, resulting in an arg288-to-pro (R288P) substitution in the basic region of the DNA-binding domain of MAF, predicted to cause an abnormal helical conformation. The cataracts were cortical pulverulent opacities in a lamellar distribution. Nuclear pulverulent opacities were present in 2 cases. Later progression with posterior subcapsular opacification necessitated surgery in adult life. Two of the 5 affected individuals had microcornea, and 1 also had bilateral iris colobomas. The mutation was not found in 217 other subjects with a range of eye anomalies or in 496 normal control chromosomes.
Wende et al. (2012) tested vibrotactile acuity over a wide range of frequencies in 4 affected members of the family originally studied by Jamieson et al. (2002). The authors found that the skin of individuals with the R288P substitution displayed reduced acuity to high-frequency vibration compared to normal controls.
In 12 affected members of a 3-generation family with congenital cerulean cataract, 6 of whom also had microcornea (CTRCT21; 610202), Vanita et al. (2006) identified heterozygosity for an 890A-G transition in the MAF gene, resulting in the replacement of a highly conserved lys297 with arg (K297R) in a basic region of the DNA-binding domain of the protein. The mutation was not found in 106 unrelated controls.
In 4 affected members spanning 3 generations of a family (CCMC0112) with cataract and microcornea (CTRCT21; 610202), Hansen et al. (2007) identified heterozygosity for a c.895C-A transversion in exon 1 of the MAF gene, resulting in an arg299-to-ser (R299S) substitution at a highly conserved residue within the alpha-helix-3 of the regulatory domain, predicted to destroy the basic region of the DNA-binding domain of the MAF leucine zipper. The mutation, which segregated with disease in the family, was not found in 152 controls. Affected individuals were diagnosed with posterior polar, nuclear lamellar, and nuclear stellate cataracts, and 1 patient also had unilateral iris coloboma.
In 6 affected members of a 3-generation Japanese family with cataract with or without microcornea (CTRCT21; 610202), Narumi et al. (2014) identified heterozygosity for a c.908A-C transversion in the MAF gene, resulting in a gln303-to-pro (Q303P) substitution at a highly conserved residue in the basic region. (Narumi et al. (2014) reported the mutation as Q303L in the abstract and on p. 1274 but as Q303P elsewhere.) The mutation, which segregated with disease in the family, was not found in 200 Japanese control alleles or in the NHLBI Exome Sequencing Project database. Affected individuals had lamellar, anterior polar, nuclear, and anterior subcapsular cataracts; additional ocular features included microcornea in 3 patients, as well as iris coloboma, mild macular hypoplasia, and retinal detachment in 1 patient each.
In 2 unrelated women with Ayme-Gripp syndrome (AYGRP; 601088), 1 of whom was originally reported by Ayme and Philip (1996), Niceta et al. (2015) identified heterozygosity for a de novo c.161C-T transition (rs727502766) in the MAF gene, resulting in a ser54-to-leu (S54L) substitution at a highly conserved residue within a GSK3 phosphorylation motif in the N-terminal transactivation domain. The mutation was not found in any of the parents. In 1 of the probands, the variant was documented in skin fibroblasts as well as hair bulb and buccal epithelial cell specimens, supporting the germline nature of the mutation. Western blot analysis of transiently transfected COS-1 cell lysates demonstrated that the S54L mutant accumulated as unphosphorylated protein, in contrast to cells expressing wildtype MAF, in which unphosphorylated MAF was barely detectable. In addition, there were increased mutant protein levels and decreased ubiquitination compared to wildtype, and treatment with cyclohexamide confirmed that the half-life of wildtype MAF was much shorter than that of the S54L mutant. Gene expression profiling analyses revealed that approximately 6% of genes in patient fibroblasts were expressed differentially compared to control fibroblasts, with an overrepresentation of genes associated with developmental programs and cellular processes. In a zebrafish model, the S54L mutation caused significant reduction in the size of the optic tectum compared to wildtype MAF, which did not induce appreciable brain volume differences.
In a 27-year-old woman with Ayme-Gripp syndrome (AYGRP; 601088), originally reported by Gripp et al. (1996), Niceta et al. (2015) identified heterozygosity for a de novo c.172A-G transition (rs727502767) in the MAF gene, resulting in a thr58-to-ala (T58A) substitution at a highly conserved residue within a GSK3 phosphorylation motif in the N-terminal transactivation domain. The mutation, which was not found in her parents, was documented in patient buccal epithelial cells, supporting the germline nature of the mutation. Western blot analysis of transiently transfected COS-1 cell lysates demonstrated that the T58A mutant accumulated as unphosphorylated protein, in contrast to cells expressing wildtype MAF, in which unphosphorylated MAF was barely detectable. In addition, there were increased mutant protein levels and decreased ubiquitination compared to wildtype, and treatment with cyclohexamide confirmed that the half-life of wildtype MAF was much shorter than that of the T58A mutant. In a zebrafish model, the T58A mutation caused significant reduction in the size of the optic tectum compared to wildtype MAF, which did not induce appreciable brain volume differences.
In a Japanese boy with Ayme-Gripp syndrome (AYGRP; 601088), originally reported by Nakane et al. (2002), Niceta et al. (2015) identified heterozygosity for a c.173C-T transition (rs727502769) in the MAF gene, resulting in a thr58-to-ile (T58I) substitution at a highly conserved residue within a GSK3 phosphorylation motif in the N-terminal transactivation domain. Parental DNA was unavailable for study. Western blot analysis of transiently transfected COS-1 cell lysates demonstrated that the T58I mutant accumulated as unphosphorylated protein, in contrast to cells expressing wildtype MAF, in which unphosphorylated MAF was barely detectable. In addition, there were increased mutant protein levels and decreased ubiquitination compared to wildtype.
In a girl with Ayme-Gripp syndrome (AYGRP; 601088), originally reported by Keppler-Noreuil et al. (2007), Niceta et al. (2015) identified heterozygosity for a de novo c.176C-A transversion (rs727502770) in the MAF gene, resulting in a pro59-to-his (P59H) substitution at a highly conserved residue within a GSK3 phosphorylation motif in the N-terminal transactivation domain. The mutation was not found in her parents. Western blot analysis of transiently transfected COS-1 cell lysates demonstrated that the P59H mutant accumulated as unphosphorylated protein, in contrast to cells expressing wildtype MAF, in which the phosphorylated protein dominated and unphosphorylated MAF was barely detectable. In addition, there were increased mutant protein levels and decreased ubiquitination compared to wildtype.
In a 5-year-old girl with Ayme-Gripp syndrome (AYGRP; 601088), Niceta et al. (2015) identified heterozygosity for a de novo c.176C-T transition (rs727502770) in the MAF gene, resulting in a pro59-to-leu (P59L) substitution at a highly conserved residue within a GSK3 phosphorylation motif in the N-terminal transactivation domain. The mutation was not found in her parents. Western blot analysis of transiently transfected COS-1 cell lysates demonstrated that the P59L mutant accumulated as unphosphorylated protein, in contrast to cells expressing wildtype MAF, in which unphosphorylated MAF was barely detectable. In addition, there were increased mutant protein levels and decreased ubiquitination compared to wildtype, and treatment with cyclohexamide confirmed that the half-life of wildtype MAF was much shorter than that of the P59L mutant. In a zebrafish model, the P59L mutation caused significant reduction in the size of the optic tectum compared to wildtype MAF, which did not induce appreciable brain volume differences.
In a 33-year-old man with Ayme-Gripp syndrome (AYGRP; 601088), originally reported by Gripp et al. (1996), Niceta et al. (2015) identified heterozygosity for a de novo c.206C-G transversion (rs727502768) in the MAF gene, resulting in a pro69-to-arg (P69R) substitution at a highly conserved residue within a GSK3 phosphorylation motif in the N-terminal transactivation domain. The mutation, which was not found in his parents, was documented in patient epithelial cells and fibroblasts, supporting the germline nature of the mutation. Western blot analysis of transiently transfected COS-1 cell lysates demonstrated that the P69R mutant showed only partial phosphorylation in contrast to cells expressing wildtype MAF, in which unphosphorylated MAF was barely detectable. In addition, there were increased mutant protein levels and decreased ubiquitination compared to wildtype, and treatment with cyclohexamide confirmed that the half-life of wildtype MAF was shorter than that of the P69R mutant. Gene expression profiling analyses revealed that approximately 6% of genes in patient fibroblasts were expressed differentially compared to control fibroblasts, with an overrepresentation of genes associated with developmental programs and cellular processes. In a zebrafish model, the P69R mutation caused significant reduction in the size of the optic tectum compared to wildtype MAF, which did not induce appreciable brain volume differences.
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