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MAF (v-maf musculoaponeurotic fibrosarcoma oncogene homolog (avian))

Identity

Other namesC-Maf
MGC71685
c-MAF
HGNC (Hugo) MAF
LocusID (NCBI) 4094
Location 16q23.2
Location_base_pair Starts at 79627745 and ends at 79634622 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order WWOX, LOC729251, MAF, DYNLRB2, CDYL2.
 

DNA/RNA

Note The MAF gene is located on chromosome 16q22-q23. Its paralogs MAFA, MAFB and NRL are located on 8q24.3, 20q11.2-q13.1 and 14q11.1-q11.2, respectively. MAF (c-MAF) was first cloned in chicken as the homolog of the founding member of the family, the viral v-MAF gene, encoded by the AS42 retrovirus that induces Musculo Aponeuorotic Fibrosarcoma (M.A.F.) in chicken. The MAF acronym originates from this tumor.
 
  The two different MAF transcripts are represented. Variant#2 corresponds to unspliced transcript. Variant#1 corresponds to alternative splicing, which contains two exons. Note that the sequence of these two exons is present on transcript variant#2.
Description The MAF gene encodes two isoforms generated through alternative splicing. These two protein isoforms are called the MAF short form and MAF long form. The MAF short form is translated from the longest mRNA (mRNA variant#2) encoded by one exon while the longest is encoded by two exons (mRNA variant#1) (see diagram). These two products differ in their carboxy terminal part, the long form containing 30 extra amino-acids.
Due to putative alternative polyadenylation signals, other transcripts might encode MAF short form.
Transcription MAF is expressed in many tissues, but its expression is lineage-specific within a given tissue. For example in T cells, MAF is expressed only in the TH2 lineage.

Protein

Note The Maf oncoproteins are b-ZIP transcription factors that belong to the AP-1 super-family, which notably includes JUN and FOS. The Maf family contains seven members, which can be subdivided into two subfamilies: the large and small Maf proteins. While the small Maf proteins, MAFF, MAFG and MAFK, are essentially composed of a b-Zip domain, the large Maf proteins, MAFA/L-MAF, MAFB, MAF/c-MAF and NRL contain an additional amino-terminal transactivation domain. Consequently, as homodimers large Maf activate transcription while small Maf repress it. Two different isoforms exist for MAF, which differ in their carboxy-terminus. The short form is constituted of 373 amino acids while the longest form contains 30 additional amino-acids. No specific function has been attributed to these two products.
 
  Schematic representation of MAF protein structure. The two different isoforms are depicted. The basic, leucine zipper, and EHR domains are indicated. The basic domain contacts directly DNA while the leucine zipper allows dimerization, which is a prerequisite for DNA binding. The EHR domain (extended homology region) is specific for the Maf proteins and is required for Maf binding to DNA. MAF protein is phosphorylated by GSK3, although the residues involved have not been formally identified. Putative GSK3 phosphorylation sites are indicated by analogy with MAFA. Phosphorylation of MAFA transactivation domain by GSK3 induces its ubiquitination and proteasome-dependent degradation. This is coupled to an increase in MAFA transactivating activity. These phosphorylations are required for MAFA transforming activity. Like MAFA and MAFB, MAF is also subjected to sumoylation, which decreases its transactivating activity. The sumoylated Lysine (K33) is indicated.
Description MAF, like all large Maf proteins, contains an amino-terminal transactivation domain and a carboxy-terminal b-ZIP DNA binding domain. Large Maf proteins stimulate transcription of their target genes through their binding to two types of palindromic sequences called TRE- or CRE- type MARE (Maf Responsive Element) (TGCTGACTCAGCA and TGCTGACGTCAGCA, respectively). The Extended Homology Region (EHR, also called ancillary domain, which is specific of the Maf proteins, allows them to recognize a longer palindromic sequence than other AP-1 family members. The MARE sequence is composed of a TRE or CRE core (underlined) flanked by a TGC sequence. While the TGC motif is crucial for Maf binding, the TRE/CRE core can be more degenerate. As other large Maf, MAF is post-translationaly modified by phosphorylation, sumoylation and ubiquitination, mostly occurring in its amino-terminal transactivation domain. Due to posttranslational modifications, notably through GSK3-mediated phosphorylation, MAF apparent molecular weight differs from the calculated one. The protein migrates as different forms ranging from 35 to 50 kDa in SDS-PAGE.
Expression MAF is expressed in many tissues including neural tissue, kidney and lens. However, its expression is lineage-specific within a given tissue. In T cells for example, MAF is expressed only in the TH2 lineage.
Localisation MAF is a nuclear protein.
Function MAF is a transcription factor of the b-Zip family that contacts DNA as homo- or hetero- dimers. MAF knockout mice show peri-natal lethality. They are microphthalmic secondary to defective lens formation. Knockout studies have revealed key roles for MAF in lens terminal differentiation where it regulates the expression of the crystallins, in the specification of the TH2 lineage by regulating the expression of the TH2-specific IL4 cytokine, as well as in chondrocyte terminal differentiation. The role of MAF in lens development is further highlighted by the existence of MAF germinal mutations responsible for congenital cataract in human.
Beside its physiological roles, MAF is an oncogene involved in human cancers (see below).
Homology MAF belongs to the AP-1 superfamilly that includes the JUN, FOS, ATF, CREB and Maf family. The Maf family is composed of seven members: the large Maf: MAF, MAFB, MAFA and NRL and the small Maf: MAFF, MAFG, MAFK that are highly homologous in their EHR- b-ZIP domains. Large Maf are closest to each others, MAF showing 77%, 67% and 53% identities with MAFB, MAFA and NRL, respectively. An ortholog of the large MAF, called TrafficJam, is found in Drosophila.

Mutations

Germinal Congenital cataract (see below)

Implicated in

Entity Multiple myeloma
Disease Multiple myeloma (cancer of plasma B cells).
Prognosis MAF translocations are of poor prognosis.
Cytogenetics t(14;16)(q32;q23).
Abnormal Protein No fusion protein. These translocations lead to the juxtaposition of a strong immunoglobulin enhancer to the MAF promoter leading to its strong ectopic expression.
Oncogenesis Large Maf proteins, MAFA, MAFB and MAF/c-MAF, are bona fide oncoproteins as demonstrated in tissue culture, animal models and in human cancer. Their oncogenic activity depends on their ability to act as transcription factors, relies on overexpression and does not require activating mutations (no such mutations have been found in human cancers), although it can be enhanced by point mutation. It is noteworthy that the transforming activity of Maf proteins is context-dependent. It is regulated by post-translational modifications, notably phosphorylation. They can occasionally display tumor suppressor-like activity in specific cellular settings. In embryonic fibroblasts, MAFA displays the strongest transforming activity. Its transforming activity depends on its phosphorylation by GSK3. In human, MAF/c-MAF, MAFB and MAFA genes are translocated to the immunoglobulin heavy chain (IgH) locus in 8-10% of multiple myelomas (MM). These translocations lead to overexpression through a strong enhancer effect without any alteration in their coding sequence. MAF translocations are present in 5% of MM. Beside these translocations, MAF is overexpressed in 50% of MM through an unknown mechanism. MAF overexpression plays a causative role in MM by promoting proliferation through cyclinD2 (CCND2) induction. It also promotes the pathological interactions of bone marrow stroma with cancer cells by enhancing integrin B7 (ITGB7) expression. These pathological cellular interactions lead to increased production of the angiogenic cytokine VEGF. MAF also activates the Ser/Thr AKT activity by inducing the expression of DEPTOR (DEPDC6), an inhibitor of mTORC1 and mTORC2 complexes.
While MM is associated with osteolytic lesions, patients with MAF deregulation show low incidence of bone disease. This observation is correlated with low expression by MAF-expressing myeloma cells of DKK1, a Wnt antagonist associated with bone disease in MM.
Chemical screens have identified glucocorticoids as potential therapeutical agents that target MAF activity through ubiquitin dependent degradation.
  
Entity Angioimmunoblastic T cell lymphoma
Prognosis Not determined.
Oncogenesis MAF has been shown to be overexpressed in 60% of angioimmunoblastic T cell lymphoma. The mechanisms underlying these deregulations are unknown. Although its causative role has not been demonstrated, its deregulation, as in multiple myeloma, is associated to that of CCND2 and ITGB7. MAF has also been found overexpressed in diverse human T cell lymphomas. Accordingly, MAF overexpression in the T cell compartment leads to T cell lymphoma associated with CCND2 and ITGB7 overexpression in transgenic mice.
  
Entity Congenital cataract
Disease In human, the MAF gene is mutated in congenital cataract that could be associated with microcornea or colomboma. These heterozygote point mutations correspond to residues located in the DNA binding domain and appear to be dominant. They disrupt DNA binding activity by targeting the different conserved basic residues R288P, K297R and R299S. Another mutation in the leucine zipper dimerization domain (K320E) was reported. In support for a role of MAF in congenital cataract, knockout studies in mice have demonstrated an important role of MAF during lens development. Moreover, heterozygote point mutants of murine MAF in its transactivation (D90V) or basic domain (R291Q, corresponding to human residue R294) lead to cataract in mice.
 
Critical residues mutated in congenital cataract in human and mice are indicated.
  

External links

Nomenclature
HGNC (Hugo)MAF   6776
Cards
AtlasMAFID41234ch16q23
Entrez_Gene (NCBI)MAF  4094  v-maf avian musculoaponeurotic fibrosarcoma oncogene homolog
GeneCards (Weizmann)MAF
Ensembl (Hinxton)ENSG00000178573 [Gene_View]  chr16:79627745-79634622 [Contig_View]  MAF [Vega]
AceView (NCBI)MAF
Genatlas (Paris)MAF
WikiGenes4094
SOURCE (Princeton)NM_001031804 NM_005360
Genomic and cartography
GoldenPath (UCSC)MAF  -  16q23.2   chr16:79627745-79634622 -  16q22-q23   [Description]    (hg19-Feb_2009)
EnsemblMAF - 16q22-q23 [CytoView]
Mapping of homologs : NCBIMAF [Mapview]
OMIM177075   610202   
Gene and transcription
Genbank (Entrez)AF055376 AF055377 AF447709 AF540388 BC038438
RefSeq transcript (Entrez)NM_001031804 NM_005360
RefSeq genomic (Entrez)AC_000148 NC_000016 NC_018927 NG_016440 NT_010498 NW_001838328 NW_004929402
Consensus coding sequences : CCDS (NCBI)MAF
Cluster EST : UnigeneHs.134859 [ NCBI ]
CGAP (NCI)Hs.134859
Alternative Splicing : Fast-db (Paris)GSHG0012005
Alternative Splicing GalleryENSG00000178573
Gene ExpressionMAF [ NCBI-GEO ]     MAF [ SEEK ]   MAF [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO75444 (Uniprot)
NextProtO75444  [Medical]
With graphics : InterProO75444
Splice isoforms : SwissVarO75444 (Swissvar)
Domaine pattern : Prosite (Expaxy)BZIP (PS50217)    BZIP_BASIC (PS00036)   
Domains : Interpro (EBI)bZIP    bZIP_Maf    Maf_TF_N    TF_DNA-bd    Transciption_factor_Maf   
Related proteins : CluSTrO75444
Domain families : Pfam (Sanger)bZIP_Maf (PF03131)    Maf_N (PF08383)   
Domain families : Pfam (NCBI)pfam03131    pfam08383   
Domain families : Smart (EMBL)BRLZ (SM00338)  
DMDM Disease mutations4094
Blocks (Seattle)O75444
Human Protein AtlasENSG00000178573
Peptide AtlasO75444
HPRD01518
IPIIPI00022438   IPI00219060   
Protein Interaction databases
DIP (DOE-UCLA)O75444
IntAct (EBI)O75444
FunCoupENSG00000178573
BioGRIDMAF
InParanoidO75444
Interologous Interaction database O75444
IntegromeDBMAF
STRING (EMBL)MAF
Ontologies - Pathways
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  chromatin  cytokine production  sequence-specific DNA binding transcription factor activity  nucleus  cytoplasm  transcription from RNA polymerase II promoter  regulation of chondrocyte differentiation  sequence-specific DNA binding  positive regulation of transcription from RNA polymerase II promoter  cell development  inner ear development  lens fiber cell differentiation  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  chromatin  cytokine production  sequence-specific DNA binding transcription factor activity  nucleus  cytoplasm  transcription from RNA polymerase II promoter  regulation of chondrocyte differentiation  sequence-specific DNA binding  positive regulation of transcription from RNA polymerase II promoter  cell development  inner ear development  lens fiber cell differentiation  
Pathways : KEGGTranscriptional misregulation in cancer    Inflammatory bowel disease (IBD)   
REACTOMEMAF
Protein Interaction DatabaseMAF
Wikipedia pathwaysMAF
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)MAF
SNP (GeneSNP Utah)MAF
SNP : HGBaseMAF
Genetic variants : HAPMAPMAF
1000_GenomesMAF 
ICGC programENSG00000178573 
Cancer Gene: CensusMAF 
Somatic Mutations in Cancer : COSMICMAF 
CONAN: Copy Number AnalysisMAF 
Mutations and Diseases : HGMDMAF
OMIM177075    610202   
GENETestsMAF
Disease Genetic AssociationMAF
Huge Navigator MAF [HugePedia]  MAF [HugeCancerGEM]
Genomic VariantsMAF  MAF [DGVbeta]
Exome VariantMAF
dbVarMAF
ClinVarMAF
snp3D : Map Gene to Disease4094
General knowledge
Homologs : HomoloGeneMAF
Homology/Alignments : Family Browser (UCSC)MAF
Phylogenetic Trees/Animal Genes : TreeFamMAF
Chemical/Protein Interactions : CTD4094
Chemical/Pharm GKB GenePA30534
Clinical trialMAF
Cancer Resource (Charite)ENSG00000178573
Other databases
Probes
Litterature
PubMed70 Pubmed reference(s) in Entrez
CoreMineMAF
iHOPMAF

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PMID 15735737
 
ARK5 is transcriptionally regulated by the Large-MAF family and mediates IGF-1-induced cell invasion in multiple myeloma: ARK5 as a new molecular determinant of malignant multiple myeloma.
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PMID 16247450
 
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Contributor(s)

Written11-2009Alain Eychène, Celio Pouponnot
Institut Curie, CNRS UMR 146, Bat110 Centre Universitaire, F-91405 Orsay, France

Citation

This paper should be referenced as such :
Eychène A, Pouponnot C . MAF (v-maf musculoaponeurotic fibrosarcoma oncogene homolog (avian)). Atlas Genet Cytogenet Oncol Haematol. November 2009 .
URL : http://AtlasGeneticsOncology.org/Genes/MAFID41234ch16q23.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/44841/1/11-2009-MAFID41234ch16q23.pdf   [ Bibliographic record ]

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indexed on : Wed Apr 16 11:19:00 CEST 2014

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