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Review
. 2011 Sep 1;3(9):a005371.
doi: 10.1101/cshperspect.a005371.

Golgi glycosylation and human inherited diseases

Hudson H Freeze  1 , Bobby G Ng
Affiliations
Review

Golgi glycosylation and human inherited diseases

Hudson H Freeze et al. Cold Spring Harb Perspect Biol. .

Abstract

The Golgi factory receives custom glycosylates and dispatches its cargo to the correct cellular locations. The process requires importing donor substrates, moving the cargo, and recycling machinery. Correctly glycosylated cargo reflects the Golgi's quality and efficiency. Genetic disorders in the specific equipment (enzymes), donors (nucleotide sugar transporters), or equipment recycling/reorganization components (COG, SEC, golgins) can all affect glycosylation. Dozens of human glycosylation disorders fit these categories. Many other genes, with or without familiar names, well-annotated pedigrees, or likely homologies will join the ranks of glycosylation disorders. Their broad and unpredictable case-by-case phenotypes cross the traditional medical specialty boundaries. The gene functions in patients may be elusive, but their common feature may include altered glycosylation that provide clues to Golgi function. This article focuses on a group of human disorders that affect protein or lipid glycosylation. Readers may find it useful to generalize some of these patient-based, translational observations to their own research.

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Figures

Figure 1.
Figure 1.
Role of the conserved oligomeric Golgi (COG) complex in Golgi localized retrograde transport. In focus is how the COG complex transports various mislocalized Golgi glycosylation proteins back to their proper destinations and then returns after redirecting the vesicles.
See this image and copyright information in PMC

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