Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases.
Standard
Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases. / Pohl, Sandra; Marschner, Katrin; Storch, Stephan; Braulke, Thomas.
in: BIOL CHEM, Jahrgang 390, Nr. 7, 7, 2009, S. 521-527.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
RIS
TY - JOUR
T1 - Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases.
AU - Pohl, Sandra
AU - Marschner, Katrin
AU - Storch, Stephan
AU - Braulke, Thomas
PY - 2009
Y1 - 2009
N2 - Abstract Lysosomes contain more than 50 soluble hydrolases that are targeted to lysosomes in a mannose 6-phosphate (Man6P)-dependent manner. The phosphorylation of man- nose residues on high mannose-type oligosaccharides of newly synthesized lysosomal enzymes is catalyzed by two multimeric enzymes, GlcNAc-1-phosphotransferase and GlcNAc-1-phosphodiester-alpha-N-acetylglucosaminidase, allowing the binding to two distinct Man6P receptors in the Golgi apparatus. Inherited defects in the GlcNAc-1-phosphotransferase complex result in missorting and cellular loss of lysosomal enzymes, and the subsequent lysosomal dysfunction causes the lysosomal storage disorders mucolipidosis types II and III. Biosynthetic studies and the availability of Man6P receptor-deficient mouse models have provided new insights into the structural requirements for preferential binding of subsets of lysosomal enzymes to Man6P receptors as well as the identification of alternative targeting pathways.
AB - Abstract Lysosomes contain more than 50 soluble hydrolases that are targeted to lysosomes in a mannose 6-phosphate (Man6P)-dependent manner. The phosphorylation of man- nose residues on high mannose-type oligosaccharides of newly synthesized lysosomal enzymes is catalyzed by two multimeric enzymes, GlcNAc-1-phosphotransferase and GlcNAc-1-phosphodiester-alpha-N-acetylglucosaminidase, allowing the binding to two distinct Man6P receptors in the Golgi apparatus. Inherited defects in the GlcNAc-1-phosphotransferase complex result in missorting and cellular loss of lysosomal enzymes, and the subsequent lysosomal dysfunction causes the lysosomal storage disorders mucolipidosis types II and III. Biosynthetic studies and the availability of Man6P receptor-deficient mouse models have provided new insights into the structural requirements for preferential binding of subsets of lysosomal enzymes to Man6P receptors as well as the identification of alternative targeting pathways.
M3 - SCORING: Zeitschriftenaufsatz
VL - 390
SP - 521
EP - 527
JO - BIOL CHEM
JF - BIOL CHEM
SN - 1431-6730
IS - 7
M1 - 7
ER -
