Animal cells and systems

The Korean Society for Integrative Biology (한국통합생물학회)
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Facilitation of SUMO (Small Ubiquitin-like Modifier) Modification at Tau 340-Lys Residue (a Microtubule-associated Protein) through Phosphorylation at 214-Ser Residue

  • Lee, Eun-Jeoung (School of Science Education, Chungbuk National University) ;
  • Hyun, Sung-Hee (Department of Pre-medicine, Eulji University School of Medicine) ;
  • Chun, Jae-Sun (Department of Biology Education, Korea National University of Education) ;
  • Ahn, Hye-Rim (School of Science Education, Chungbuk National University) ;
  • Kang, Sang-Sun (School of Science Education, Chungbuk National University)
  • Published : 2007.06.30
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Abstract

Tau plays a role in numerous neuronal processes, such as vesicle transport, microtubule-plasma membrane interaction and intracellular localization of proteins. SUMO (Small Ubiquitin-like Modifier) modification (SUMOylation) appears to regulate diverse cellular processes including nuclear transport, signal transduction, apoptosis, autophagy, cell cycle control, ubiquitin-dependent degradation, as well as gene transcription. We noticed that putative SUMOylation site is localized at $^{340}K$ of $Tau(^{339}VKSE^{342})$ with the consensus sequence information (${\Phi}KxE$ ; where ${\Phi}$ represents L, I, V or F and x is any amino acid). In this report, we demonstrated that $^{340}K$ of Tau is the SUMOylation site and that a point mutant of Tau S214E (an analog of the phospho $^{214}S$ Tau) promotes its SUMOylation at $^{340}K$ and its nuclear or nuclear vicinity localization, by co-immunoprecipitation and confocal microscopy analysis. Further, we demonstrate that the Tau S214E (neither Tau S214A nor Tau K340R) mutant increases its protein stability. However, the SUMOylation at $^{340}K$ of Tau did not influence cell survival, as determined by FACS analysis. Therefore, our results suggested that the phosphorylation of Tau on $^{214}S$ residue promotes its SUMOylation on $^{340}K$ residue and nuclear vicinity localization, and increases its stability, without influencing cell survival.

Keywords

References

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