PMID: 20044576

 

    Legend: Gene, Sites

Title : O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding

Abstract :

1. Alpha-dystroglycan ( alpha-DG ) is a cell-surface glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains and certain arenaviruses
2. Receptor binding is thought to be mediated by a posttranslational modification, and defective binding with laminin underlies a subclass of congenital muscular dystrophy
3. Using mass spectrometry- and nuclear magnetic resonance (NMR)-based structural analyses, we identified a phosphorylated O-mannosyl glycan on the mucin-like domain of recombinant alpha- DG, which was required for laminin binding
4. We demonstrated that patients with muscle-eye-brain disease and Fukuyama congenital muscular dystrophy, as well as mice with myodystrophy, commonly have defects in a postphosphoryl modification of this phosphorylated O-linked mannose, and that this modification is mediated by the like-acetylglucosaminyltransferase ( LARGE ) protein
5. These findings expand our understanding of the mechanisms that underlie congenital muscular dystrophy

Output (sent_index, trigger, protein, sugar, site):

• 1. glycoprotein, , glycoprotein, Alpha-dystroglycan, -
• 1. glycoprotein, , receptor, Alpha-dystroglycan, -
• 3. glycan, , -, the mucin-like domain, domain
• 3. glycan, , DG,, glycan, -

Output(Part-Of) (sent_index, protein, site):

• 1. laminin, domains
• 1. proteins, domains
• 3. DG,, domain

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
DG,	1605	3