novel protein that physically interacts with Suppressor of Hairless and the intracellular domain of Notch that is produced upon receptor activation - functions as a transcriptional coactivator for Notch signaling
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.50
1596 (aa); 167 (kD predicted)
The protein has many AA homomeric domains: 21 poly-Gln runs (from 5 to 16 AA in length), 4 poly-Gly (6 to 10 AA), 3 poly-Asn (3 X 5 AA), 1 poly-Ala (10 AA) and 1 poly-Thr (5 AA) runs.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\mam using the Feature Mapper tool.
The nuclear localization of mam protein is consistent with its proposed role in gene regulation. Early in embryogenesis, mam protein shows nuclear, punctate localization. Immunohistochemical studies show that mam protein binds to more than 100 locations on polytene chromosomes, some of which colocalize with a subset of RNA polymerase and gro protein binding sites.
The pattern of mam protein localization is comparable to that of mam transcript. During gastrulation, the highest levels of mam protein are found in the ventral furrow, although expression is also seen in the cephalic furrow. Late in gastrulation, mam protein accumulates in the mesoderm and in the midgut primordia. At the completion of gastrulation, there are high levels of mam protein in the mesectoderm, the neurectoderm, as well as in the midgut primordia and the cephalic furrow.
GBrowse - Visual display of RNA-Seq signalsView Dmel\mam in GBrowse 2
Determined by deletion mapping.
Please 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.
The N signaling pathway is important for the formation and maintenance of the germline stem cell niche in the ovary.
RNAi generated by PCR using primers directed to this gene causes a cell growth and viability phenotype when assayed in Kc167 and S2R+ cells.
2 alleles of mam have been isolated in a genetic screen for autosomal mutations that produce blisters in somatic wing clones.
mam protein is widely expressed during embryonic and postembryonic development. Within salivary glands mam protein binds to over 100 polytene chromosome sites. Comparison of mams basic domain sequence to known proteins suggest that it may be distantly related to a subset of the leucine zipper class of transcription factors.
mam is a neurogenic gene required initially to ensure the correct number of PNS precursors. mam continues to be required in the peripheral ectoderm, possibly for maintenance of the commitment to an epidermal fate.
NM1 defines a new class of Notch allele: similarity with and lack of specificity of interaction of N- and NM1 with H, mam, gro and E(spl) suggest that the NM1 effect is due to modification in the intracellular signalling of the activated N receptor.
The embryonic phenotype of neurogenic mutations was examined in most tissues using Ecol\lacZ enhancer trap lines. All alleles examined show defects in many organs from all three germ layers. At least for ectodermally and endodermally derived tissues, neurogenic gene function is primarily involved in interactions among cells that need to acquire or maintain an epithelial phenotype.
The expression of mam RNA and protein during embryogenesis (up to the completion of gastrulation) has been studied.
mam is needed for proper mesoderm differentiation prior to the onset of nau expression: mutant alleles cause hypertrophy in nau expressing cells.
Mutations of mam, bib and neur in an heterozygous condition had no effect on the expression of NAx-59d or NAx-59b except when coupled in cis with Nfa-g. The neurogenic mutations suppress the wing venation phenotype of N.
mam alleles act as enhancers of spl alleles of N.
An extra wild type copy of mam, in combination with dxENU, causes some pupal lethality, escapers have small eyes.
Analysis of N and mam mutant combinations reveals that reduction of the wild type number of mam was capable of interferring with the mechanism underlying negative complementation in a manner that was not restricted to specific Abruptex combinations.
Neural hyperplasia, caused by mutations in mam, can be prevented by the presence of another neurogenic mutation.
Regions of mam cross-hybridize to the opa sequence.
mam has been molecularly cloned.
Homozygous embryonic lethal; embryos display neural hyperplasia with compensatory epidermal hypoplasia; caused by failure of most ventral ectodermal cells to differentiate as epidermal cells rather than neuroblasts, as seen in N, amx, bib, neu, Dl, and E(spl); mam tends to have less extreme neural hyperplasia than mutants at the other neurogenic loci. A similar diversion of cells from epidermigenic into neurogenic pathways seen to generate supernumerary peripheral nerve cells (Hartenstein and Campos-Ortega, 1986). When mam expressed in female germ cells and the ensuing embryos, neural hyperplasia is enhanced, but mam+ embryos from oocytes are normal (Jimenez and Campos Ortega, 1982). Homozygous clones in the eye display irregular ommatidial pattern characterized by lack of interommatidial bristles, enlarged facets with supernumerary retinular cells and reduced numbers of pigment cells; in the cuticle, clones homozygous for mam2 are devoid of bristles (Dietrich and Campos-Ortega, 1984). mam1 (formerly N-2G) heterozygotes occasionally exhibit apical wing nicking; not recorded for other alleles. Phenotype of homozygotes for null allele reduced by duplications for normal alleles of other neurogenic loci, N, neu, Dl, E(spl) and H, but not amx or bib (de la Concha et al., 1988).