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Gene Review

flw  -  flapwing

Drosophila melanogaster

Synonyms: CG15305, CG2096, DmPp1-9C, Dmel\CG2096, FLW, ...
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High impact information on flw

  • In contrast, expression of transgenes encoding the Bif F995A mutant, which disrupts binding to PP1, was unable to rescue any aspect of the bif phenotype [1].
  • The gene bifocal (bif), required for photoreceptor morphogenesis in the Drosophila compound eye, encodes a protein that is shown to interact with protein phosphatase 1 (PP1) using the yeast two-hybrid system [1].
  • 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] [2].
  • Furthermore, human activated Aurora-A forms complexes with the negative regulator protein serine/threonine phosphatase type 1 (PP1) that was negatively phosphorylated on Thr320 [3].
  • PP1beta9C interacts with Trithorax in Drosophila wing development [4].

Biological context of flw

  • PP1beta9C was found to be present at all TRX sites on the polytene chromosomes [4].
  • The gene for Drosophila PP1 beta is localized at 9C1-2 on the X chromosome and encodes a protein of 330 amino acids with a predicted molecular mass of 37.8 kDa [5].
  • The sequence of Drosophila PP1 alpha 1 was deduced from a 2.2-kb cDNA purified from an embryonic cDNA library, while that for Drosophila PP1 beta was obtained from overlapping clones isolated from both a head cDNA library and an eye imaginal disc cDNA library [5].
  • Metazoans from Drosophila to humans have multiple genes encoding catalytic subunits of PP1 (PP1c), which are involved in a wide range of biological processes [6].
  • Drosophila is an excellent model organism in which to characterize the role of PP1 catalytic and regulatory subunits, because it combines molecular and biochemical approaches with powerful genetics, in a well-characterized animal model [6].

Anatomical context of flw


Associations of flw with chemical compounds

  • A construct encoding PP1beta9C with a short NH(2)-terminal fusion including six histidine residues was introduced into the X-33 and KM71H strains of P. pastoris by homologous recombination [7].

Other interactions of flw

  • Direct binding was demonstrated by GST pull-down experiments and PP1beta9C/TRX interaction in vivo was confirmed by coimmune precipitation from Drosophila embryonic extracts [4].

Analytical, diagnostic and therapeutic context of flw

  • PP1beta9C was purified to a specific activity of 12,077 mU/mg by a three-step purification method comprising (NH(4))(2)SO(4)-ethanol precipitation followed by Ni(2+)-agarose affinity chromatography and Mono Q anion-exchange chromatography [7].


  1. Interaction with protein phosphatase 1 Is essential for bifocal function during the morphogenesis of the Drosophila compound eye. Helps, N.R., Cohen, P.T., Bahri, S.M., Chia, W., Babu, K. Mol. Cell. Biol. (2001) [Pubmed]
  2. Protein phosphatase 1beta is required for the maintenance of muscle attachments. Raghavan, S., Williams, I., Aslam, H., Thomas, D., Szöor, B., Morgan, G., Gross, S., Turner, J., Fernandes, J., VijayRaghavan, K., Alphey, L. Curr. Biol. (2000) [Pubmed]
  3. Phospho-regulation of human protein kinase Aurora-A: analysis using anti-phospho-Thr288 monoclonal antibodies. Ohashi, S., Sakashita, G., Ban, R., Nagasawa, M., Matsuzaki, H., Murata, Y., Taniguchi, H., Shima, H., Furukawa, K., Urano, T. Oncogene (2006) [Pubmed]
  4. PP1beta9C interacts with Trithorax in Drosophila wing development. Rudenko, A., Bennett, D., Alphey, L. Dev. Dyn. (2004) [Pubmed]
  5. Drosophila contains three genes that encode distinct isoforms of protein phosphatase 1. Dombrádi, V., Axton, J.M., Brewis, N.D., da Cruz e Silva, E.F., Alphey, L., Cohen, P.T. Eur. J. Biochem. (1990) [Pubmed]
  6. Yeast Two-Hybrid Screens to Identify Drosophila PP1-Binding Proteins. Bennett, D., Alphey, L. Methods Mol. Biol. (2006) [Pubmed]
  7. Biochemical characterization of recombinant Drosophila type 1 serine/threonine protein phosphatase (PP1c) produced in Pichia pastoris. Szöor, B., Gross, S., Alphey, L. Arch. Biochem. Biophys. (2001) [Pubmed]
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