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protein glycosylation


- The majority of proteins that traverse the secretory pathway receive asparagine (Asn)-linked glycosylations.

- Glycans are bulky hydrophilic modifications that serve a variety of structural and functional roles within the cell.

- The role of Asn-linked glycans is proteic maturation and quality-control protein tags in the early secretory pathway.

- The carbohydrate composition encodes crucial information about the structure, localization and age of glycoproteins.

- The "glycan code" is encoded by a series of glycosidases and carbohydrate transferases that line the secretory pathway.

- This code is deciphered by carbohydrate-binding proteins that possess distinct carbohydrate binding properties and act as molecular chaperones or sorting receptors.

- These glycosidases and transferases work in concert with resident secretory pathway carbohydrate-binding proteins to form a network that assists in the maturation and trafficking of both native and aberrant glycoproteins within the cell.

See also

- protein maturation

Video

References

- Martin PT. Congenital muscular dystrophies involving the O-mannose pathway. Curr Mol Med. 2007 Jun;7(4):417-25. PMID: 17584082

- Rampal R, Luther KB, Haltiwanger RS. Notch signaling in normal and disease States: possible therapies related to glycosylation. Curr Mol Med. 2007 Jun;7(4):427-45. PMID: 17584081

- Schulz BL, Laroy W, Callewaert N. Clinical laboratory testing in human medicine based on the detection of glycoconjugates. Curr Mol Med. 2007 Jun;7(4):397-416. PMID: 17584080

- Freeze HH. Congenital Disorders of Glycosylation: CDG-I, CDG-II, and beyond. Curr Mol Med. 2007 Jun;7(4):389-96. PMID: 17584079

- Freeze HH.Novel perspectives on glycosylation and human disease. Curr Mol Med. 2007 Jun;7(4):387. PMID: 17584078

- Hebert DN, Garman SC, Molinari M. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 2005 Jul;15(7):364-70. PMID: 15939591

- Grewal PK, Hewitt JE. Glycosylation defects: a new mechanism for muscular dystrophy? Hum Mol Genet. 2003 Oct 15;12 Spec No 2:R259-64. PMID: 12925572