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Gene Review

mts  -  microtubule star

Drosophila melanogaster

Synonyms: 5559, CG7109, DmPp2A-28D, Dmel\CG7109, ER2-6, ...
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Disease relevance of mts

  • A Drosophila strain, carrying a P[lacW] element in the promoter of the protein phosphatase 2A (PP2A) catalytic subunit gene at chromosomal location 28D, has been identified using plasmid rescue of the P element and adjoining genomic DNA in Escherichia coli [1].
  • Reduction of PP2A activity reduces PER expression in central clock neurons and results in long periods and arrhythmia [2].
  • Treatment of extracts from human breast cancer (MCF7) cells with either alkali or ethanol increased immunoreactivity of PP2Ac subunit severalfold on Western blots with Ab299/309, but did not apparently change molecular weight or isoelectric point of the protein [3].
  • Finally, some viral proteins such as adenovirus E4orf4 and simian virus small t target PP2A to alter its activity, resulting in induction of apoptosis as a regulatory mechanism to enhance virus spread [4].

High impact information on mts


Biological context of mts


Anatomical context of mts

  • This suggests that polarized PP2A activation along the planar microtubule web is important for planar polarization [7].
  • Multiple centrosomes are visible in cellularised embryos, suggesting that PP2A may play a role in coupling the nuclear and centrosome cycles [1].
  • Although information about the signaling pathways present in Drosophila S2 cells is not as well developed as many mammalian cell lines, the Drosophila system is particularly attractive for the study of oligomeric phosphatases like PP2A [10].

Associations of mts with chemical compounds


Other interactions of mts


  1. Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos. Snaith, H.A., Armstrong, C.G., Guo, Y., Kaiser, K., Cohen, P.T. J. Cell. Sci. (1996) [Pubmed]
  2. Posttranslational regulation of Drosophila PERIOD protein by protein phosphatase 2A. Sathyanarayanan, S., Zheng, X., Xiao, R., Sehgal, A. Cell (2004) [Pubmed]
  3. The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. Favre, B., Zolnierowicz, S., Turowski, P., Hemmings, B.A. J. Biol. Chem. (1994) [Pubmed]
  4. Phosphatases in apoptosis: to be or not to be, PP2A is in the heart of the question. Van Hoof, C., Goris, J. Biochim. Biophys. Acta (2003) [Pubmed]
  5. Protein phosphatase 2A positively and negatively regulates Ras1-mediated photoreceptor development in Drosophila. Wassarman, D.A., Solomon, N.M., Chang, H.C., Karim, F.D., Therrien, M., Rubin, G.M. Genes Dev. (1996) [Pubmed]
  6. Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits. Silverstein, A.M., Barrow, C.A., Davis, A.J., Mumby, M.C. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  7. Planar cell polarization requires Widerborst, a B' regulatory subunit of protein phosphatase 2A. Hannus, M., Feiguin, F., Heisenberg, C.P., Eaton, S. Development (2002) [Pubmed]
  8. The regulatory subunits of fission yeast protein phosphatase 2A (PP2A) affect cell morphogenesis, cell wall synthesis and cytokinesis. Kinoshita, K., Nemoto, T., Nabeshima, K., Kondoh, H., Niwa, H., Yanagida, M. Genes Cells (1996) [Pubmed]
  9. Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster. Nowak, S.J., Pai, C.Y., Corces, V.G. Mol. Cell. Biol. (2003) [Pubmed]
  10. Analysis of protein phosphatase function in Drosophila cells using RNA interference. Silverstein, A.M., Mumby, M.C. Meth. Enzymol. (2003) [Pubmed]
  11. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Janssens, V., Goris, J. Biochem. J. (2001) [Pubmed]
  12. The phosphatase subunit tap42 functions independently of target of rapamycin to regulate cell division and survival in Drosophila. Cygnar, K.D., Gao, X., Pan, D., Neufeld, T.P. Genetics (2005) [Pubmed]
  13. Protein phosphatase 2A as a new target for morphogenetic studies in the chick limb. Viallet, J., Garcia, A., Weydert, A. Biochimie (2003) [Pubmed]
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