Thursday 27 January 2005
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 carbohydrate composition encodes crucial information about the structure, localization and age of glycoproteins.
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.
< object width="425" height="350"> < param name="movie" value="http://www.youtube.com/v/G33cD2YleRI"> < /param> < param name="wmode" value="transparent"> < /param> < embed src="http://www.youtube.com/v/G33cD2YleRI" type="application/x-shockwave-flash" wmode="transparent" width="425" height="350"> < /embed> < /object>
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
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