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Gene Review

Ote  -  Otefin

Drosophila melanogaster

Synonyms: CG5581, Dmel\CG5581, hal, ote, otefin
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High impact information on Ote

  • Our results suggest that interactions with lamin might mediate or stabilize the localization of otefin and YA in the nuclear lamina [1].
  • The ubiquitous major lamina protein, lamin Dm, interacts with both otefin, a peripheral protein of the inner nuclear membrane, and YA, an essential, developmentally regulated protein of the nuclear lamina [1].
  • Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA [1].
  • Lamin's rod domain interacts with the complete otefin protein, with otefin's hydrophilic NH2-terminal domain, and with two different fragments derived from this domain [1].
  • In agreement with this interaction, lamin and otefin can be coimmunoprecipitated from the vesicle fraction of Drosophila embryos and colocalize in nuclear envelopes of Drosophila larval salivary gland nuclei [1].

Biological context of Ote


Anatomical context of Ote


Associations of Ote with chemical compounds


Co-localisations of Ote

  • With the exception of sperm cells, otefin colocalizes with lamin Dm0 derivatives in situ and presumably in vivo and is present in all somatic cells examined during the different stages of Drosophila development [2].

Other interactions of Ote

  • The population that interacts first with chromatin contains lamin and otefin and requires both peripheral and integral membrane proteins, whereas fusion of vesicles requires GTPase activity [5].
  • These chromatin-attached vesicles contained lamin Dm and otefin but not gp210 [5].
  • Of all putative Drosophila LEM-domain proteins, otefin and Bocksbeutel exhibited the highest similarity in the LEM motif (53% identical amino acids) [6].


  1. Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA. Goldberg, M., Lu, H., Stuurman, N., Ashery-Padan, R., Weiss, A.M., Yu, J., Bhattacharyya, D., Fisher, P.A., Gruenbaum, Y., Wolfner, M.F. Mol. Cell. Biol. (1998) [Pubmed]
  2. Localization and posttranslational modifications of otefin, a protein required for vesicle attachment to chromatin, during Drosophila melanogaster development. Ashery-Padan, R., Ulitzur, N., Arbel, A., Goldberg, M., Weiss, A.M., Maus, N., Fisher, P.A., Gruenbaum, Y. Mol. Cell. Biol. (1997) [Pubmed]
  3. Isolation and characterization of the Drosophila nuclear envelope otefin cDNA. Padan, R., Nainudel-Epszteyn, S., Goitein, R., Fainsod, A., Gruenbaum, Y. J. Biol. Chem. (1990) [Pubmed]
  4. Persistence of major nuclear envelope antigens in an envelope-like structure during mitosis in Drosophila melanogaster embryos. Harel, A., Zlotkin, E., Nainudel-Epszteyn, S., Feinstein, N., Fisher, P.A., Gruenbaum, Y. J. Cell. Sci. (1989) [Pubmed]
  5. Nuclear membrane vesicle targeting to chromatin in a Drosophila embryo cell-free system. Ulitzur, N., Harel, A., Goldberg, M., Feinstein, N., Gruenbaum, Y. Mol. Biol. Cell (1997) [Pubmed]
  6. Two novel LEM-domain proteins are splice products of the annotated Drosophila melanogaster gene CG9424 (Bocksbeutel). Wagner, N., Schmitt, J., Krohne, G. Eur. J. Cell Biol. (2004) [Pubmed]
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