Open AccessGlycosylation defects corrected by the changes in GDPmannose level.
Author(s) -
Joanna S. Kruszewska,
A. Janik,
Urszula Lenart,
Grażyna Palamarczyk
Publication year - 1999
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1999_4165
Subject(s) - dolichol , glycoprotein , endoplasmic reticulum , glycosylation , golgi apparatus , mannose , biochemistry , oligosaccharide , saccharomyces cerevisiae , glycan , chemistry , biosynthesis , yeast , microbiology and biotechnology , biology , enzyme
GDPMan is a key substrate in glycoprotein formation. This is especially true for lower eukaryotes where, in addition to the involvement in N-glycan biosynthesis and GPI-anchor formation, GDPMan takes part in the process which is unique for yeast and fungi i.e. O-mannosylation. Several lines of evidence have been presented that the level of GDPMan affects the process occurring in the Golgi compartment i.e. the elongation of outer mannose chain of glycoproteins in Saccharomyces cerevisiae. Results from our laboratory indicate that the availability of GDPMan affects also the early steps of glycoprotein formation ascribed to the endoplasmic reticulum, i.e. assembly of the dolichol-linked oligosaccharide as well as mannosyl-phosphodolichol (MPD) formation. The biochemical basis of carbohydrate deficient glycoprotein syndrome, a severe neurological disorder related to the GDPMan deficiency, is also discussed.