Journal
HUMAN MUTATION
Volume 30, Issue 12, Pages 1628-1641Publisher
WILEY
DOI: 10.1002/humu.21126
Keywords
glycosylation; endoplasmic reticulum; CDG; dolichol; glycoprotein
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Funding
- Korber Foundation
- Swiss National Science Foundation [31003A-116039]
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Defects in the biosynthesis of the oligosaccharide precursor for N-glycosylation lead to decreased occupancy of glycosylation sites and thereby to diseases known as congenital disorders of glycosylation (CDG). In the last 20 years, approximately 1,000 CDG patients have been identified presenting with multiple organ dysfunctions. This review sets the state of the art by listing all mutations identified in the 15 genes (PMM2, MPI, DPAGT1, ALG1, ALG2, ALG3, ALG9, ALG12, ALG6, ALG8, DOLK, DPM1, DPM3, MPDU1, and RFT1) that yield a deficiency of dolichol-linked oligosaccharide biosynthesis. The present analysis shows that most mutations lead to substitutions of strongly conserved amino acid residues across eukaryotes. Furthermore, the comparison between the different forms of CDG affecting dolichol-linked oligosaccharide biosynthesis shows that the severity of the disease does not relate to the position of the mutated gene along this biosynthetic pathway. Hum Mutat 30:1628-1641, 2009. (C) 2009 Wiley-Liss, Inc.
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