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Gene Review

Act87E  -  Actin 87E

Drosophila melanogaster

Synonyms: Act87e, Actin, Actin-87E, CG18290, Dmel\CG18290, ...
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Disease relevance of Act87E


Psychiatry related information on Act87E

  • These findings raise the possibility that a direct interaction between tau and actin may be a critical mediator of tau-induced neurotoxicity in Alzheimer's disease and related disorders [3].

High impact information on Act87E

  • However, DmIKK epsilon-mediated degradation of DIAP1 does not regulate apoptosis as might be predicted but instead regulates actin dynamics, cell morphology, and the differentiation of sensory organ precursor cells [6].
  • These composite data define three main patterns of actin gene expression which are correlated with changing Drosophila morphology, particularly muscle differentiation and reorganization [7].
  • Furthermore, the messages encoding alpha-tubulin, beta-tubulin, and actin are found associated with one-third to one-half as many total ribosomes in heat-shocked cells as in cells incubated at 25 degrees C. Increased temperature should lead to increased output of protein per ribosome [8].
  • Each of the approximately 30,000 wing epithelial cells constructs an actin-rich prehair that protrudes from its distal vertex and points distally [9].
  • These include proteins that participate in haemocyte development, vesicle transport, actin cytoskeleton regulation and a cell surface receptor [10].

Biological context of Act87E

  • The Act87E transcription unit is 1.57 kb and includes a 556-base intervening sequence in the 5' leader of the gene [11].
  • By in situ hybridization with a series of deficiencies that break in 87E, Act87E was localized to a region encompassing one to three faint, polytene chromosome bands [11].
  • The lower density of negative charge in subdomain 1 of actin therefore weakens the actomyosin interaction sufficiently to decrease the force and motion generating capacity of E99K actin, thus providing the primary insult that ultimately leads to the disease phenotype [1].
  • Here we have addressed how two actin regulators, capping protein, a barbed end binding protein, and the Arp2/3 complex, a potent actin assembly nucleator, function to generate properly organized bundles [12].
  • The implications of the failure to identify recessive lethal mutations in the actin gene are discussed in reference to studies of other conserved multigene families and other muscle protein mutations [11].

Anatomical context of Act87E

  • Drosophila melanogaster bristle development is dependent on actin assembly, and prominent actin bundles form against the elongating cell membrane, giving the adult bristle its characteristic grooved pattern [12].
  • In salivary glands and follicle cells the head and neck domains were concentrated in the cell nucleus, where the minus end of each actin filament is located [13].
  • An intron at codon 150 is common to a plant actin gene and the skeletal muscle acting gene [14].
  • If, however, Drosophila mRNA was translated in a mRNA-dependent rabbit reticulocyte lysate system, an additional 43-kDa actin intermediate was observed [15].
  • Myosin VI stabilizes an actin network during Drosophila spermatid individualization [16].

Associations of Act87E with chemical compounds

  • These data confirm that N-acetyl-cysteine at the N terminus affects actomyosin interactions, probably by reducing formation of the initial actomyosin collision complex, a process known to involve the actin N terminus [17].
  • Our results show that ACT88F is N-terminally processed in vivo as a class II actin by removal of the first two amino acid residues (Met and Cys), but that uniquely the N terminus is not acetylated [17].
  • The cDNA encoding the entire RVGP gene was cloned in an expression plasmid under the control of the constitutive actin promoter (Ac), which was co-transfected into S2 cells together with a hygromycin selection plasmid [18].
  • Intron positions typical of other known plant actin genes are conserved in these clones [19].
  • The removal of Ac-Cys from Drosophila actin is thus similar to removal of Ac-Met from the NH2 terminus of class I actins although in the case of the class II actins, it is the second amino acid that is removed as an acetylated species [15].

Physical interactions of Act87E

  • We interpret these results as possibly caused either by effects on A1 myosin light chain binding or conformational changes within the subdomain 1 of actin, which contains the myosin binding site [20].
  • Biochemical studies showed that both ninaC proteins bind actin filaments and cosediment with actin filaments in an ATP-sensitive manner [21].

Enzymatic interactions of Act87E

  • Previous studies with Drosophila actin showed that the first detectable intermediate is one with an Ac-Cys NH2 terminus which is subsequently cleaved in a novel reaction to expose the Asp [22].

Other interactions of Act87E

  • Actomyosin kinetics and in vitro motility of wild-type Drosophila actin and the effects of two mutations in the Act88F gene [20].
  • In a time- and acetyl-CoA-dependent fashion, Met-Cys-Asp-actin was processed to the mature actin, presumably through an Ac-Met-Cys-Asp intermediate [22].
  • These results outline structural roles for the ninaC proteins, and are consistent with the notion, suggested by their amino acid sequences, that the proteins are actin-based mechanoenzymes [21].
  • Germ-line armadillo mutations appear to disrupt processes requiring cell adhesion and integrity of the actin cytoskeleton, consistent with a role for Armadillo in cell-cell adhesive junctions [23].
  • In nurse cells that contain excess quail but no fascin, the cytoplasmic actin network initially appears wild type but then becomes disorganized in the final stages of nurse cell cytoplasm transport [24].

Analytical, diagnostic and therapeutic context of Act87E

  • Sequence analysis of the indirect flight muscle actin-encoding gene of Drosophila simulans [25].
  • Purification entails lysis in a low salt, sucrose buffer that contains ATP, chromatography on DEAE-cellulose, precipitation with actin in the absence of ATP, gel filtration in a discontinuous KI-KCl buffer system, and hydroxylapatite chromatography [26].
  • Similarly, in Drosophila, actin and myosin 2 localization and cell constriction at the margin of the epidermis mediate dorsal closure and are controlled by Misshapen [27].
  • Actin-myosin structures align across multiple cells during rosette formation, and adherens junction proteins assemble in a stepwise fashion during rosette resolution [28].
  • With the use of a pulse-chase protocol and two-dimensional gel electrophoresis, it has been found that actin III is synthesized as a precursor of the more stable cytoplasmic actin II [29].


  1. Functional consequences of a mutation in an expressed human alpha-cardiac actin at a site implicated in familial hypertrophic cardiomyopathy. Bookwalter, C.S., Trybus, K.M. J. Biol. Chem. (2006) [Pubmed]
  2. Left-right asymmetry: class I myosins show the direction. Spéder, P., Noselli, S. Curr. Opin. Cell Biol. (2007) [Pubmed]
  3. Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Fulga, T.A., Elson-Schwab, I., Khurana, V., Steinhilb, M.L., Spires, T.L., Hyman, B.T., Feany, M.B. Nat. Cell Biol. (2007) [Pubmed]
  4. Epstein-Barr virus infection induces expression in B lymphocytes of a novel gene encoding an evolutionarily conserved 55-kilodalton actin-bundling protein. Mosialos, G., Yamashiro, S., Baughman, R.W., Matsudaira, P., Vara, L., Matsumura, F., Kieff, E., Birkenbach, M. J. Virol. (1994) [Pubmed]
  5. Stage-specific expression of two actin genes in the yellow fever mosquito, Aedes aegypti. Vyazunova, I., Lan, Q. Insect Mol. Biol. (2004) [Pubmed]
  6. A kinase gets caspases into shape. Montell, D.J. Cell (2006) [Pubmed]
  7. Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Fyrberg, E.A., Mahaffey, J.W., Bond, B.J., Davidson, N. Cell (1983) [Pubmed]
  8. The control of protein synthesis during heat shock in Drosophila cells involves altered polypeptide elongation rates. Ballinger, D.G., Pardue, M.L. Cell (1983) [Pubmed]
  9. Fidelity in planar cell polarity signalling. Ma, D., Yang, C.H., McNeill, H., Simon, M.A., Axelrod, J.D. Nature (2003) [Pubmed]
  10. Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Rämet, M., Manfruelli, P., Pearson, A., Mathey-Prevot, B., Ezekowitz, R.A. Nature (2002) [Pubmed]
  11. Molecular and genetic characterization of the Drosophila melanogaster 87E actin gene region. Manseau, L.J., Ganetzky, B., Craig, E.A. Genetics (1988) [Pubmed]
  12. Capping protein and the Arp2/3 complex regulate nonbundle actin filament assembly to indirectly control actin bundle positioning during Drosophila melanogaster bristle development. Frank, D.J., Hopmann, R., Lenartowska, M., Miller, K.G. Mol. Biol. Cell (2006) [Pubmed]
  13. The expression pattern and cellular localisation of Myosin VI during the Drosophila melanogaster life cycle. Millo, H., Bownes, M. Gene Expr. Patterns (2007) [Pubmed]
  14. Nucleotide sequence of the rat skeletal muscle actin gene. Zakut, R., Shani, M., Givol, D., Neuman, S., Yaffe, D., Nudel, U. Nature (1982) [Pubmed]
  15. NH2-terminal processing of Drosophila melanogaster actin. Sequential removal of two amino acids. Rubenstein, P.A., Martin, D.J. J. Biol. Chem. (1983) [Pubmed]
  16. Myosin VI stabilizes an actin network during Drosophila spermatid individualization. Noguchi, T., Lenartowska, M., Miller, K.G. Mol. Biol. Cell (2006) [Pubmed]
  17. Drosophila ACT88F indirect flight muscle-specific actin is not N-terminally acetylated: a mutation in N-terminal processing affects actin function. Schmitz, S., Clayton, J., Nongthomba, U., Prinz, H., Veigel, C., Geeves, M., Sparrow, J. J. Mol. Biol. (2000) [Pubmed]
  18. Rabies virus glycoprotein expression in Drosophila S2 cells. I. Functional recombinant protein in stable co-transfected cell line. Yokomizo, A.Y., Jorge, S.A., Astray, R.M., Fernandes, I., Ribeiro, O.G., Horton, D.S., Tonso, A., Tordo, N., Pereira, C.A. Biotechnology journal (2007) [Pubmed]
  19. A complex gene superfamily encodes actin in petunia. Baird, W.V., Meagher, R.B. EMBO J. (1987) [Pubmed]
  20. Actomyosin kinetics and in vitro motility of wild-type Drosophila actin and the effects of two mutations in the Act88F gene. Anson, M., Drummond, D.R., Geeves, M.A., Hennessey, E.S., Ritchie, M.D., Sparrow, J.C. Biophys. J. (1995) [Pubmed]
  21. Role of the ninaC proteins in photoreceptor cell structure: ultrastructure of ninaC deletion mutants and binding to actin filaments. Hicks, J.L., Liu, X., Williams, D.S. Cell Motil. Cytoskeleton (1996) [Pubmed]
  22. Alternate pathways for removal of the class II actin initiator methionine. Martin, D.J., Rubenstein, P.A. J. Biol. Chem. (1987) [Pubmed]
  23. A role for the Drosophila segment polarity gene armadillo in cell adhesion and cytoskeletal integrity during oogenesis. Peifer, M., Orsulic, S., Sweeton, D., Wieschaus, E. Development (1993) [Pubmed]
  24. Drosophila fascin mutants are rescued by overexpression of the villin-like protein, quail. Cant, K., Knowles, B.A., Mahajan-Miklos, S., Heintzelman, M., Cooley, L. J. Cell. Sci. (1998) [Pubmed]
  25. Sequence analysis of the indirect flight muscle actin-encoding gene of Drosophila simulans. Beifuss, M.J., Durica, D.S. Gene (1992) [Pubmed]
  26. Cytoplasmic myosin from Drosophila melanogaster. Kiehart, D.P., Feghali, R. J. Cell Biol. (1986) [Pubmed]
  27. Coordinated cell-shape changes control epithelial movement in zebrafish and Drosophila. Köppen, M., Fernández, B.G., Carvalho, L., Jacinto, A., Heisenberg, C.P. Development (2006) [Pubmed]
  28. Multicellular rosette formation links planar cell polarity to tissue morphogenesis. Blankenship, J.T., Backovic, S.T., Sanny, J.S., Weitz, O., Zallen, J.A. Dev. Cell (2006) [Pubmed]
  29. A precursor of cytoplasmic actin in cultured Drosophila cells. Berger, E., Cox, G. J. Cell Biol. (1979) [Pubmed]
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