Post-translational modifications of the gamma-subunit affect intracellular trafficking and complex assembly of GlcNAc-1-phosphotransferase.

@article{Encarnao2011PosttranslationalMO,
  title={Post-translational modifications of the gamma-subunit affect intracellular trafficking and complex assembly of GlcNAc-1-phosphotransferase.},
  author={Marisa Encarnaç{\~a}o and Katrin Kollmann and Maria Trusch and Thomas Braulke and Sandra Pohl},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 7},
  pages={5311-8}
}
GlcNAc-1-phosphotransferase plays a key role in the generation of mannose 6-phosphate, a recognition marker essential for efficient transport of lysosomal hydrolases to lysosomes. The enzyme complex is composed of six subunits (α(2)β(2)γ(2)). The α- and β-subunits are catalytically active, whereas the function of the γ-subunit is still unclear. We have investigated structural properties, localization, and intracellular transport of the human and mouse γ-subunits and the molecular requirements… CONTINUE READING