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Gene Review

zip  -  zipper

Drosophila melanogaster

Synonyms: CG15792, DROMHC, Dm nmII, Dmel\CG15792, DmnmII, ...
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Disease relevance of zip

  • To investigate this regulation in a complex eukaryote, we purified the Drosophila myosin-II tail expressed in Escherichia coli and showed that it was phosphorylated in vitro by protein kinase C(PKC) at serines 1936 and 1944, which are located in the nonhelical globular tail piece [1].
  • Planar polarization of the denticle field in the Drosophila embryo: Roles for Myosin II (Zipper) and Fringe [2].
  • Temperature-sensitive mutations in the myosin domain resulted in retinal degeneration, but no ERG phenotype [3].
  • Here we show that Wolbachia infection results in increased mRNA and protein expression of the Drosophila simulans nonmuscle myosin II gene zipper [4].
  • We have identified partial loss of function mutations in class VI unconventional myosin, 95F myosin, which results in male sterility [5].

Psychiatry related information on zip


High impact information on zip

  • The role of myosin II in mitosis is generally thought to be restricted to cytokinesis [7].
  • Myosin II-dependent cortical movement is required for centrosome separation and positioning during mitotic spindle assembly [7].
  • Latex beads bound to the cell surface move in a myosin II-dependent manner in the direction of the separating asters [7].
  • The primary output of Drok signaling is regulating the phosphorylation of nonmuscle myosin regulatory light chain, and hence the activity of myosin II [8].
  • The slbo locus was found to encode a product homologous to the CCAAT/enhancer-binding protein (C/EBP), a basic region-leucine zipper transcription factor [9].

Biological context of zip

  • Mutations of zip, which encodes the nonmuscle myosin heavy chain, suppress the phenotypes of rib and raw, suggesting that rib and raw are not directly required for myosin function [10].
  • The F-actin based motor protein myosin II has a key role in cytokinesis [11].
  • Taken together, this genetic evidence argues that phosphorylation at serine-21 is critical to RMLC function in activating myosin II in vivo, but that the function can be partially provided by phosphorylation at threonine-20 [12].
  • These findings confirm that p127 is a component of a cytoskeletal network including myosin and suggest that the neoplastic transformation resulting from l(2)gl gene inactivation may be caused by the partial disruption of this network [13].
  • Drosophila nonmuscle myosin II has multiple essential roles in imaginal disc and egg chamber morphogenesis [14].

Anatomical context of zip

  • The cortical myosin cycle does not require microtubules but correlates inversely with Cdc2/cyclinB (mitosis-promoting factor) activity [15].
  • The ring canals, cytoplasmic bridges linking the oocyte to the nurse cells in the egg chamber, are abnormal, suggesting a role of myosin II in their establishment or maintenance [12].
  • In addition, numerous aggregates of myosin heavy chain accumulate in the sqh null cells [12].
  • We show that embryos that lack zygotic expression of nonmuscle myosin-II fail to form striated myofibrils [16].
  • We suggest that nonmuscle myosin-II functions at the muscle termini and the Z-line as an actin crosslinker and acts to maintain the structural integrity of the sarcomere [16].

Associations of zip with chemical compounds

  • We find that nonmuscle myosin-II and the adhesion molecule, PS2 integrin, colocalize at the developing muscle termini [16].
  • They show that arrestin is carried into the light-sensitive microvilli by phosphoinositide-enriched vesicles driven by a myosin motor [17].
  • Mutation of either or both of these sites to alanine did not effect the ability of Cdc4p to bind the type II myosin Myo2p, and cells expressing only these mutated versions of Cdc4p grew and divided normally [18].
  • To determine the function of myosin-II in these cells, retinal tissue was incubated with 2,3-butanedione 2-monoxime (BDM), an inhibitor of myosin activity [19].
  • We found that the Schneider cells undergo myogenic differentiation upon treatment with neocarzinostatin (NCS), DNA double-strand break (DSB)-inducing drug, as indicated by elongated morphology, myosin heavy chain protein expression, multinucleation and exit from the cell cycle [20].

Physical interactions of zip


Regulatory relationships of zip


Other interactions of zip


Analytical, diagnostic and therapeutic context of zip

  • DRhoGEF2 exerts its effects in gastrulation through the regulation of Myosin II to orchestrate coordinated apical cell constriction [25].
  • Biochemical and cell culture analyses suggest that Rho signal transduction regulates the activity of myosin [26].
  • Flies also contain a cytoplasmic myosin heavy chain polypeptide that by immunological and peptide mapping criteria is clearly different from the major thoracic muscle isoform [27].
  • Sequence analysis of genomic DNA identifies the lesion responsible for zipIIF107, one of the original severe embryonic lethal zipper alleles [28].
  • Immobilization of cortical movement with tetravalent lectins produces similar spindle defects to myosin II disruption and suggests that myosin II activity is required within the cortex [7].


  1. Protein kinase C phosphorylates nonmuscle myosin-II heavy chain from Drosophila but regulation of myosin function by this enzyme is not required for viability in flies. Su, Z., Kiehart, D.P. Biochemistry (2001) [Pubmed]
  2. Planar polarization of the denticle field in the Drosophila embryo: Roles for Myosin II (Zipper) and Fringe. Walters, J.W., Dilks, S.A., Dinardo, S. Dev. Biol. (2006) [Pubmed]
  3. Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis. Porter, J.A., Montell, C. J. Cell Biol. (1993) [Pubmed]
  4. Induced paternal effects mimic cytoplasmic incompatibility in Drosophila. Clark, M.E., Heath, B.D., Anderson, C.L., Karr, T.L. Genetics (2006) [Pubmed]
  5. Class VI unconventional myosin is required for spermatogenesis in Drosophila. Hicks, J.L., Deng, W.M., Rogat, A.D., Miller, K.G., Bownes, M. Mol. Biol. Cell (1999) [Pubmed]
  6. Modes of protein movement that lead to the asymmetric localization of partner of Numb during Drosophila neuroblast division. Lu, B., Ackerman, L., Jan, L.Y., Jan, Y.N. Mol. Cell (1999) [Pubmed]
  7. Myosin II-dependent cortical movement is required for centrosome separation and positioning during mitotic spindle assembly. Rosenblatt, J., Cramer, L.P., Baum, B., McGee, K.M. Cell (2004) [Pubmed]
  8. Drosophila Rho-associated kinase (Drok) links Frizzled-mediated planar cell polarity signaling to the actin cytoskeleton. Winter, C.G., Wang, B., Ballew, A., Royou, A., Karess, R., Axelrod, J.D., Luo, L. Cell (2001) [Pubmed]
  9. slow border cells, a locus required for a developmentally regulated cell migration during oogenesis, encodes Drosophila C/EBP. Montell, D.J., Rorth, P., Spradling, A.C. Cell (1992) [Pubmed]
  10. ribbon, raw, and zipper have distinct functions in reshaping the Drosophila cytoskeleton. Blake, K.J., Myette, G., Jack, J. Dev. Genes Evol. (1999) [Pubmed]
  11. Type II myosin regulatory light chain relieves auto-inhibition of myosin-heavy-chain function. Naqvi, N.I., Wong, K.C., Tang, X., Balasubramanian, M.K. Nat. Cell Biol. (2000) [Pubmed]
  12. Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosophila. Jordan, P., Karess, R. J. Cell Biol. (1997) [Pubmed]
  13. The Drosophila lethal(2)giant larvae tumor suppressor protein forms homo-oligomers and is associated with nonmuscle myosin II heavy chain. Strand, D., Jakobs, R., Merdes, G., Neumann, B., Kalmes, A., Heid, H.W., Husmann, I., Mechler, B.M. J. Cell Biol. (1994) [Pubmed]
  14. Drosophila nonmuscle myosin II has multiple essential roles in imaginal disc and egg chamber morphogenesis. Edwards, K.A., Kiehart, D.P. Development (1996) [Pubmed]
  15. Cortical recruitment of nonmuscle myosin II in early syncytial Drosophila embryos: its role in nuclear axial expansion and its regulation by Cdc2 activity. Royou, A., Sullivan, W., Karess, R. J. Cell Biol. (2002) [Pubmed]
  16. zipper Nonmuscle myosin-II functions downstream of PS2 integrin in Drosophila myogenesis and is necessary for myofibril formation. Bloor, J.W., Kiehart, D.P. Dev. Biol. (2001) [Pubmed]
  17. Myosin III illuminates the mechanism of arrestin translocation. Strissel, K.J., Arshavsky, V.Y. Neuron (2004) [Pubmed]
  18. Phosphorylation of the myosin-II light chain does not regulate the timing of cytokinesis in fission yeast. McCollum, D., Feoktistova, A., Gould, K.L. J. Biol. Chem. (1999) [Pubmed]
  19. Distribution of nonmuscle myosin-II in honeybee photoreceptors and its possible role in maintaining compound eye architecture. Baumann, O. J. Comp. Neurol. (2001) [Pubmed]
  20. Myogenic differentiation of Drosophila Schneider cells by DNA double-strand break-inducing drugs. Hossain, M.S., Akimitsu, N., Kurokawa, K., Sekimizu, K. Differentiation (2003) [Pubmed]
  21. Anillin binds nonmuscle myosin II and regulates the contractile ring. Straight, A.F., Field, C.M., Mitchison, T.J. Mol. Biol. Cell (2005) [Pubmed]
  22. Drosophila myosin phosphatase and its role in dorsal closure. Mizuno, T., Tsutsui, K., Nishida, Y. Development (2002) [Pubmed]
  23. Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complexes. Berrios, M., Fisher, P.A., Matz, E.C. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  24. Cap 'n' collar B cooperates with a small Maf subunit to specify pharyngeal development and suppress deformed homeotic function in the Drosophila head. Veraksa, A., McGinnis, N., Li, X., Mohler, J., McGinnis, W. Development (2000) [Pubmed]
  25. A Rho GTPase signaling pathway is used reiteratively in epithelial folding and potentially selects the outcome of Rho activation. Nikolaidou, K.K., Barrett, K. Curr. Biol. (2004) [Pubmed]
  26. Genetic analysis demonstrates a direct link between rho signaling and nonmuscle myosin function during Drosophila morphogenesis. Halsell, S.R., Chu, B.I., Kiehart, D.P. Genetics (2000) [Pubmed]
  27. Identification of the gene for fly non-muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family. Kiehart, D.P., Lutz, M.S., Chan, D., Ketchum, A.S., Laymon, R.A., Nguyen, B., Goldstein, L.S. EMBO J. (1989) [Pubmed]
  28. Molecular organization and alternative splicing in zipper, the gene that encodes the Drosophila non-muscle myosin II heavy chain. Mansfield, S.G., al-Shirawi, D.Y., Ketchum, A.S., Newbern, E.C., Kiehart, D.P. J. Mol. Biol. (1996) [Pubmed]
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