Disease relevance of fliI

• Transgenic flies that express Act88F with either a 6x histidine tag or an 11-residue peptide derived from vesicular stomatitis virus G protein at the C terminus were flightless [1].

High impact information on fliI

• At the Drosophila larval neuromuscular junction, amphiphysin is localized postsynaptically and amphiphysin mutants have no major defects in neurotransmission; they are also viable, but flightless [2].
• By comparing the structure of wild-type and mutant muscle myosin heavy chain (MHC) genes of Drosophila melanogaster, we have identified the defect in the homozygous-viable, flightless mutant Mhc10 [3].
• However, rod polypeptides interfere with muscle function and cause a flightless phenotype [4].
• We find that haploidy of TmI causes myofibrillar disruptions and flightless behavior, but that haploidy of TmII causes neither [5].
• Introduction of a transformed copy of the wild type MLC-2 gene rescues the dominant flightless behavior of Mlc2E38 heterozygotes [6].

Biological context of fliI

• Mutations at the flightless-I locus (fliI) of Drosophila melanogaster cause flightlessness or, when severe, incomplete cellularization during early embryogenesis, with subsequent abnormalities in mesoderm invagination and in gastrulation [7].
• After chromosome walking, deficiency mapping, and transgenic analysis, we have isolated and characterized flightless-I cDNAs, enabling prediction of the complete amino acid sequence of the 1256-residue protein [7].
• Data transferability from model organisms to human beings: insights from the functional genomics of the flightless region of Drosophila [8].
• There is a strong possibility that ligands for this group could be related and that flightless may have a similar role in Ras signal transduction [9].
• Conversely, comparison of 24 amino acid sequences of LRR proteins including the flightless proteins indicates that flightless proteins are members of a structurally related subgroup [9].

Anatomical context of fliI

• The structure of the maternally expressed flightless-I protein suggests that it may play a key role in embryonic cellularization by interacting with both the cytoskeleton and other cellular components [7].
• The Drosophila melanogaster flightless I gene is required for normal cellularization of the syncytial blastoderm [10].
• These mutations cause a dominant flightless phenotype but allow relatively normal assembly of indirect flight muscle myofibrils [11].
• Expression of the truncated DMLC2 rescues the recessive lethality and dominant flightless phenotype of the Dmlc2 null, with no discernible effect on indirect flight muscle (IFM) sarcomere assembly [12].
• A large number of dominant flightless mutants of Drosophila were chemically induced, and their thorax proteins were examined by chemically induced, and their thorax proteins were examined by means of two-dimensional gel electrophoresis (O'Farrell 1975) [13].

Associations of fliI with chemical compounds

• The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans [7].
• After mutagenesis with ethyl methanesulphonate (EMS), we screened for X-linked flightless mutants of Drosophila melanogaster by using column-type flight tester [14].
• Here, we show that Drosophila mutants for the inositol 1,4,5-trisphosphate (InsP(3)) receptor gene (itpr) are flightless [15].

Regulatory relationships of fliI

• Exchanging the flight muscle-specific exon 3 region into the embryonic isoform increased actin sliding velocity 3-fold and improved indirect flight muscle ultrastructure integrity but failed to rescue the flightless phenotype of flies expressing embryonic myosin [16].

Other interactions of fliI

• We report here that tweety, a gene located in Drosophila flightless, has a structure similar to those of known channels and that human homologues of tweety (hTTYH1-3) are novel maxi-Cl(-) channels. hTTYH3 mRNA was found to be distributed in excitable tissues [17].
• We have analysed the developmental defects in Drosophila embryos lacking a gelsolin-related protein encoded by the gene flightless I [18].
• The presence of four copies of Mhc results in overabundance of the protein and a flightless phenotype [19].
• We show that PP1beta9C corresponds to flapwing (flw), previously identified mutants of which are viable but flightless because of defects in indirect flight muscles (IFMs) [8] [20].
• As canB2 is an essential gene and rare homozygous escapers are flightless, we further analyzed canB2 expression and function in pupae and adults [21].

Analytical, diagnostic and therapeutic context of fliI

• We have used a combination of histological, molecular, and genetic techniques to investigate the flightless Drosophila mutant raised [22].
• Sequence analysis of the cDNAs revealed that clone 93A represents a previously unidentified gene, clone 98C has homology to an expressed sequence tag from goat mammary tissue, and clone 200A is identical to the human homologue of the Drosophila melanogaster flightless-I gene [23].
• We used a Drosophila melanogaster flightless mutant Ifm(3)3 and a genetic cross of this mutant with wild type flies to achieve a gradation of tropomyosin gene dosage [24].

References