Journal
JOURNAL OF PROTEOME RESEARCH
Volume 11, Issue 8, Pages 3955-3964Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr200996y
Keywords
O-glycans; O-mannosylation; neurofascin; dystroglycan; O-glycosylation; ESI-MS; GC-MS
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Funding
- Deutsche Forschungsgemeinschaft [BR 3979/1-1, HA 2092/15-1]
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Protein O-mannosylation is an important modification in mammals, and deficiencies thereof lead to a variety of severe phenotypes. Although it has already been shown that the amount of O-mannosyl glycans in brain is very high, only very few proteins have been identified as O-mannosylated. Additionally, the functions of the O-mannose-based glycans are still speculative and only investigated for alpha-dystroglycan. In a previous study a cis-located peptide was identified, which controls O-mannosylation in mammals. A BLAST search on the basis of this peptidic determinant identified other potential O-mannosylated proteins. Among these neurofascin was chosen for further analysis as a recombinant probe (mucin domain) and as an endogenous protein from mouse brain. Mass spectrometric data for both proteins confirmed that neurofascin186 is indeed O-mannosylated. Glycopeptide analysis by liquid chromatography-tandem mass spectrometry allowed for the identification of some of the O-mannosylation sites, which are not restricted to the mucin domain but were found also within N-terminal IgG and Fibronectin domains of the protein.
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