<p>Intracellular sorting of most soluble lysosomal enzymes occurs by tagging with mannose 6-phosphate (M6P) residues in the Golgi apparatus allowing recognition by M6P-receptors and transport to lysosomes. GlcNAc-1-phosphotransferase (GNPT) catalyzes the first step in M6P-tagging. Although the M6P sorting pathway is well-studied and was thought to be completely understood, several novel regulators of GNPT localization and stabilization in the cis-Golgi apparatus have been recently identified.</p>

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Neue Regulatoren des Mannose-6-Phosphat-abhängigen Proteintransportwegs

  • Zilei Chen,
  • Anna La Rosa,
  • Sabrina Jabs

摘要

Intracellular sorting of most soluble lysosomal enzymes occurs by tagging with mannose 6-phosphate (M6P) residues in the Golgi apparatus allowing recognition by M6P-receptors and transport to lysosomes. GlcNAc-1-phosphotransferase (GNPT) catalyzes the first step in M6P-tagging. Although the M6P sorting pathway is well-studied and was thought to be completely understood, several novel regulators of GNPT localization and stabilization in the cis-Golgi apparatus have been recently identified.