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Gene Review

smt3  -  CG4494 gene product from transcript CG4494-RA

Drosophila melanogaster

Synonyms: CG4494, Dm0342, DmSUMO-1, DmSmt3, Dmel\CG4494, ...
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High impact information on smt3

  • Post-translational modification of proteins by the ubiquitin-like molecule SUMO (sumoylation) regulates their subcellular localization and affects their functional properties in vitro, but the physiological function of sumoylation in multicellular organisms is largely unknown [1].
  • SUMO modification of Sp3 occurs at a single lysine located between the second glutamine-rich activation domain and the DNA-binding domain [2].
  • We demonstrate that Tramtrack 69 (Ttk69), a repressor of neuronal differentiation, is a bona fide in vivo substrate for dSmt3 conjugation [3].
  • Altogether, these data indicate a high conservation of the Smt3 conjugation pathway and further suggest that this mechanism may play a role in the transcriptional regulation of cell differentiation in Drosophila flies [3].
  • In the presence of Ulp1, most SUMO conjugates reside in the nucleus [4].

Biological context of smt3


Anatomical context of smt3


Associations of smt3 with chemical compounds

  • The conjugation of the ubiquitin-like protein SUMO to lysine side chains plays widespread roles in the regulation of nuclear protein function [8].

Physical interactions of smt3

  • We have found that DmUbc9 binds and conjugates Drosophila Smt3 (DmSmt3) to Dorsal [10].

Other interactions of smt3

  • We did not observe any concentration of DmUba2 at sites where the septins are concentrated, and we could not detect DmSmt3 modification of the three Drosophila septins tested [6].
  • We found that at least one isoform of Drosophila neuronal CaMKII is conjugated to DmSUMO-1 in vivo [7].
  • The effect of DmUbc9 on Dorsal activity was potentiated by the overexpression of DmSmt3 [10].
  • We found that flies heterozygous for a deficiency uncovering vestigial (vg) and mutations in any of several genes encoding components of the SUMO conjugation machinery exhibit severe wing notching [8].


  1. SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2. Zhang, H., Smolen, G.A., Palmer, R., Christoforou, A., van den Heuvel, S., Haber, D.A. Nat. Genet. (2004) [Pubmed]
  2. Transcription factor Sp3 is silenced through SUMO modification by PIAS1. Sapetschnig, A., Rischitor, G., Braun, H., Doll, A., Schergaut, M., Melchior, F., Suske, G. EMBO J. (2002) [Pubmed]
  3. Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies. Lehembre, F., Badenhorst, P., Müller, S., Travers, A., Schweisguth, F., Dejean, A. Mol. Cell. Biol. (2000) [Pubmed]
  4. Drosophila Ulp1, a nuclear pore-associated SUMO protease, prevents accumulation of cytoplasmic SUMO conjugates. Smith, M., Bhaskar, V., Fernandez, J., Courey, A.J. J. Biol. Chem. (2004) [Pubmed]
  5. Ras1 interacts with multiple new signaling and cytoskeletal loci in Drosophila eggshell patterning and morphogenesis. Schnorr, J.D., Holdcraft, R., Chevalier, B., Berg, C.A. Genetics (2001) [Pubmed]
  6. Identification of septin-interacting proteins and characterization of the Smt3/SUMO-conjugation system in Drosophila. Shih, H.P., Hales, K.G., Pringle, J.R., Peifer, M. J. Cell. Sci. (2002) [Pubmed]
  7. Identification and characterization of a SUMO-1 conjugation system that modifies neuronal calcium/calmodulin-dependent protein kinase II in Drosophila melanogaster. Long, X., Griffith, L.C. J. Biol. Chem. (2000) [Pubmed]
  8. SUMO enhances vestigial function during wing morphogenesis. Takanaka, Y., Courey, A.J. Mech. Dev. (2005) [Pubmed]
  9. Systematic, RNA-interference-mediated identification of mus-101 modifier genes in Caenorhabditis elegans. Holway, A.H., Hung, C., Michael, W.M. Genetics (2005) [Pubmed]
  10. A functional interaction between dorsal and components of the Smt3 conjugation machinery. Bhaskar, V., Valentine, S.A., Courey, A.J. J. Biol. Chem. (2000) [Pubmed]
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