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Gene Review

Mtor  -  Megator

Drosophila melanogaster

Synonyms: Bx34, CG8274, Dmel\CG8274, MTOR, Nuclear envelope antigen Bx34, ...
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High impact information on Mtor

  • The TPR snap helix: a novel protein repeat motif from mitosis to transcription [1].
  • However, during mitosis Megator reorganizes and aligns together with Skeletor and Chromator into a fusiform spindle structure [2].
  • During interphase Megator is localized to the nuclear rim and occupies the intranuclear space surrounding the chromosomes [2].
  • On the basis of these findings we propose that the COOH-terminal domain of Megator functions as a targeting and localization domain, whereas the NH2-terminal domain is responsible for forming polymers that may serve as a structural basis for the putative spindle matrix complex [2].
  • The Megator metaphase spindle persists in the absence of microtubule spindles, strongly implying that the existence of the Megator-defined spindle does not require polymerized microtubules [2].

Biological context of Mtor


Anatomical context of Mtor


Associations of Mtor with chemical compounds


Other interactions of Mtor


Analytical, diagnostic and therapeutic context of Mtor

  • However, we show by immunoprecipitation experiments that EAST is likely to molecularly interact with Megator which has a large NH2-terminal coiled-coil domain with the capacity for self assembly [5].
  • This is supported by the fact that in yeast two hybrid assays the tetratricopeptide repeat E (TPR E) of Rols7 shows interaction with the intracellular domain of Duf/Kirre [8].


  1. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. Goebl, M., Yanagida, M. Trends Biochem. Sci. (1991) [Pubmed]
  2. Megator, an essential coiled-coil protein that localizes to the putative spindle matrix during mitosis in Drosophila. Qi, H., Rath, U., Wang, D., Xu, Y.Z., Ding, Y., Zhang, W., Blacketer, M.J., Paddy, M.R., Girton, J., Johansen, J., Johansen, K.M. Mol. Biol. Cell (2004) [Pubmed]
  3. A Drosophila Tpr protein homolog is localized both in the extrachromosomal channel network and to nuclear pore complexes. Zimowska, G., Aris, J.P., Paddy, M.R. J. Cell. Sci. (1997) [Pubmed]
  4. Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition. Chung, S., McLean, M.R., Rymond, B.C. RNA (1999) [Pubmed]
  5. EAST interacts with Megator and localizes to the putative spindle matrix during mitosis in Drosophila. Qi, H., Rath, U., Ding, Y., Ji, Y., Blacketer, M.J., Girton, J., Johansen, J., Johansen, K.M. J. Cell. Biochem. (2005) [Pubmed]
  6. Drosophila crooked-neck protein co-fractionates in a multiprotein complex with splicing factors. Raisin-Tani, S., Léopold, P. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  7. Control of triglyceride storage by a WD40/TPR-domain protein. Häder, T., Müller, S., Aguilera, M., Eulenberg, K.G., Steuernagel, A., Ciossek, T., Kühnlein, R.P., Lemaire, L., Fritsch, R., Dohrmann, C., Vetter, I.R., Jäckle, H., Doane, W.W., Brönner, G. EMBO Rep. (2003) [Pubmed]
  8. Drosophila Rolling pebbles colocalises and putatively interacts with alpha-Actinin and the Sls isoform Zormin in the Z-discs of the sarcomere and with Dumbfounded/Kirre, alpha-Actinin and Zormin in the terminal Z-discs. Kreisköther, N., Reichert, N., Buttgereit, D., Hertenstein, A., Fischbach, K.F., Renkawitz-Pohl, R. J. Muscle Res. Cell. Motil. (2006) [Pubmed]
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