SLC30A3 (ZnT3) Oligomerization by Dityrosine Bonds Regulates Its Subcellular Localization and Metal Transport Capacity

@article{Salazar2009SLC30A3O,
  title={SLC30A3 (ZnT3) Oligomerization by Dityrosine Bonds Regulates Its Subcellular Localization and Metal Transport Capacity},
  author={Gloria P{\'e}rez Salazar and Juan Manuel Falc{\'o}n-P{\'e}rez and Robert Harrison and Victor Faundez},
  journal={PLoS ONE},
  year={2009},
  volume={4},
  pages={38 - 47}
}
Non-covalent and covalent homo-oligomerization of membrane proteins regulates their subcellular localization and function. Here, we described a novel oligomerization mechanism affecting solute carrier family 30 member 3/zinc transporter 3 (SLC30A3/ZnT3). Oligomerization was mediated by intermolecular covalent dityrosine bonds. Using mutagenized ZnT3 expressed in PC12 cells, we identified two critical tyrosine residues necessary for dityrosine-mediated ZnT3 oligomerization. ZnT3 carrying the… CONTINUE READING
21 Extracted Citations
57 Extracted References
Similar Papers

Citing Papers

Publications influenced by this paper.
Showing 1-10 of 21 extracted citations

Referenced Papers

Publications referenced by this paper.
Showing 1-10 of 57 references

Improved Parameters for Generating Partial Charges: Correlation with Observed Dipole Moments’

  • P Bagossi, G Zahuczky, J T, W I.T, H R.W
  • J Mol Model
  • 1999
Highly Influential
5 Excerpts

Dominantnegative AT2 receptor oligomers induce G-protein arrest and symptoms of neurodegeneration

  • S Abdalla, H Lother, A El Missiry, P Sergeev, A Langer
  • J Biol Chem
  • 2008
1 Excerpt

Similar Papers

Loading similar papers…