pMad, Mothers Against Decapentaplegic, dMad, Smad, Mother against decapentaplegic
Smad family members convey TGFß signals from their receptors to the nucleus - Upon phosphorylation by either Sax or Tkv (type I BMP receptors), Mad forms a complex with Med and translocates to the nucleus where, together with cofactors, it regulates expression of BMP response target genes.
Please see the JBrowse view of Dmel\Mad for information on other features
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AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.45
Gene model reviewed during 5.46
Tissue-specific extension of 3' UTRs observed during later stages (FBrf0218523, FBrf0219848); all variants may not be annotated
2.6 (northern blot)
None of the polypeptides share 100% sequence identity.
455 (aa)
Homotrimer (PubMed:19557331). Interacts with MAN1 (PubMed:20036230). Interacts with Sec13 and Nup93-1 (PubMed:20547758).
Phosphorylation on Ser-453 and/or Ser-455 is required for interaction with Smurf (PubMed:12754252, PubMed:18327897). Phosphorylation on Ser-25 by key/Nemo promotes export from nucleus and antagonizes BMP signaling (PubMed:17507407).
Ubiquitinated by Smurf upon phosphorylation; which promotes proteasomal degradation.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Mad using the Feature Mapper tool.
Comment: maternally deposited
Mad 2.6kb transcripts are detected in all developmental stages but are most abundant in early embryos, pupae, and adult females. A minor slightly smaller transcript is also detected in 0-4hr embryos.
Comment: antibody against phosphorylated form
Comment: antibody against phosphorylated form
Comment: in primordial germ cell (PGC), at mid-third instar (ML3, 96hr AEL)
Comment: antibody specific to phosphorylated Mad
Comment: antibody specific to phosphorylated Mad
Comment: antibody specific to phosphorylated Mad (pMad)
Comment: antibody specific to phosphorylated Mad (pMad)
Comment: antibody specific to phosphorylated Mad (pMad)
Comment: 23-26 hr APF
Comment: high expression level
Comment: low expression level
Comment: anti-phosphorylated Mad antibody
pMad is expressed in CCAP-EN neurons but not in the CCAP-IN neurons.
In the eye disc, antibody to phosphorylated Mad stains a broad band of cells anterior to and within the morphogenetic furrow, terminating in a stripe of more intensely labelled cells around columns 3 and 4 at the posterior edge of the furrow. In antennal disc, a broad band of nuclei in the ventral region of the disc is stained. Staining is observed in peripodial cells over the ventral region of the antennal disc and the dorsal region of the eye disc. In some preparations, nuclear pMad was also weakly detected in peripodial epithelium cells directly overlying the morphogenetic furrow.
Phosphorylated Mad protein is expressed in the presynaptic domain of type I boutons at the neuromuscular junction.
Phosphorylated Mad (pMAd) protein is detected in the spiracular chambers, spiracular branches, and dorsal trunk branches of the tracheal system. Expression is seen in the spiracular chamber form embryonic stage 13 and appears in the spriacular branch and dorsal trunk branches at stage 14 and persists through stage 17.
Mad is observed in the dorsal epidermis and the ventrolateral epidermis at embryonic stage 13.
Phosphorylated Mad (pMad) is detected in the amnioserosa and in the epidermis around the leading edge at embryonic stage 11. A ventral stripe is also seen. From stage 12 on, pMad levels decline in the amnioserosa but persist in epidermis stripes. At doral closure, expression is absent from the amnioserosa but persists in the epidermis.
Phosphorylated Mad protein is detected in centripetal follicle cells.
In third instar larval eye discs, the phosphorylated form of Mad is observed in a low-level, uniform granular distribution in and anterior to the morphogenetic furrow. Expression rises to a high level in regular groups of cells on the posterior side for two columns. This is followed by very low-level expression further posterior. The highest levels appear in groups of cells, just posterior to the first and second column of single ato-positive ommatidial founder cells and posterior to dpp transcription as revealed by a dpp lacZ reporter.
Strong pMad staining is observed in the
precursor cells of the longitudinal veins around 19-22 hr after pupation. From 17-22 hr APF, pMAD accumulates in a broad patch of cells in the region of the presumptive posterior crossvein. During subsequent stages (13-28 hr APF), the pMAD staining becomes refined into a narrow stripe of cells that form the posterior crossvein.
Phosphorylated Mad protein is distributed in a gradient, with the highest levels near the anterior/posterior compartment boundary.
staining was for for pMad
In male adults, Mad protein is expressed in germline stem cells.
In female adults, Mad protein is expressed at a high level in germline stem cells, and at a low level in cystoblasts.
Phosphorylated Mad protein is localized to a subset of motor neurons in late stage embryos.
Phosphorylated Mad (pMad) is first detected at future sites of the crossveins at 19-21 hr APF and in portions of the longitudinal veins near the crossvein attachment sites and along wing vein L2. By 24-26 hr APF staining is seen all along the longitudinal veins but is stronger near the crossveins. At 36 hr APF, staining is seen throughout the wing but is stronger in the crossveins. Strong staining is also observed in the nuclei and axons of the PNS of the wing at 18-36 hr APF.
Mad protein is ubiquitously distributed in embryos.
GBrowse - Visual display of RNA-Seq signals
View Dmel\Mad in GBrowse 2Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
polyclonal
monoclonal
polyclonal antibody
Source for merge of: E(zen)2 Mad
Source for merge of: Mad l(2)k00237
Source for merge of: Mad apg
DNA-protein interactions: genome-wide binding profile assayed for Mad protein in stage 9-11 embryos; ArrayExpress accession number E-MTAB-1184.
DNA-protein interactions: genome-wide binding profile assayed for Mad protein in 2-3 hr embryos; see BDTNP1_TFBS_Mad collection report.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
Hsap\MADH1 and Hsap\MADH4, as well as Mad and Med, can stimulate dpp signalling in limb development.
Overexpression of Mad or Hsap\MADH1 in the wing and leg causes a similar phenotype.
Mutants show no interaction with Df(2R)Pcl11B or Df(3L)66C-G28.
Mutants isolated in a screen of the second chromosome identifying genes affecting disc morphology.
The amino-terminal domain of the Mad protein contains a sequence-specific DNA-binding activity that becomes apparent when carboxy-terminal residues are removed. Mad protein binds to and is required for the activation of an enhancer within the vg gene in cells across the entire developing wing blade.
Mad is required for any response of the visceral mesoderm or endoderm to dpp signals from the visceral mesoderm and is required specifically in cells responding to dpp. Mad can function in the signalling pathway of BMP-4 in Xenopus embryos, and is thus a highly conserved and essential element of the dpp signalling pathway.
Mad is required for dpp signalling during eye development. Clonal analysis demonstrated that this requirement is cell autonomous. Mad is an essential component of the signal transduction pathway downstream of the dpp receptors in responding cells. Mad-mediated dpp signaling is absolutely required for the initiation of the morphogenetic furrow in the eye, but has only a minor role in its subsequent propagation across the eye disc.
Dominant enhancer of zen.
Mad has been identified independently in two screens, one for dominant enhancers of the dpp mutant phenotype and dosage sensitive interactions with dpp. Mad mutant phenotypes show patterning defects that resemble many dpp mutant phenotypes. Studies of ectopic expression, tissue-specific expression and in situ hybridizations are consistent with a role for Mad downstream of dpp in the signalling pathway.
A genetic enhancer of dpp.
The gene is named "apang" after the mutant phenotype ("apang" stands for an individual with mutilated and underdeveloped legs in Hindi).