O-glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues
O-mannosylation is a vital protein modification. In humans, defective O-mannosylation of α-dystroglycan results in severe congenital muscular dystrophies. However, other proteins bearing this modification in vivo are still largely unknown. Here, we describe a highly reliable method combining glycosi...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
7 October 2013
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| In: |
FEBS letters
Year: 2013, Volume: 587, Issue: 22, Pages: 3715-3721 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2013.09.041 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1016/j.febslet.2013.09.041 Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2013.09.041/epdf 
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| Author Notes: | Patrick R. Winterhalter, Mark Lommel, Thomas Ruppert, Sabine Strahl |
| Summary: | O-mannosylation is a vital protein modification. In humans, defective O-mannosylation of α-dystroglycan results in severe congenital muscular dystrophies. However, other proteins bearing this modification in vivo are still largely unknown. Here, we describe a highly reliable method combining glycosidase treatment with LC-MS analyses to identify mammalian O-mannosylated proteins from tissue sources. Our workflow identified T-cadherin (H-cadherin, CDH13) as a novel O-mannosylated protein. In contrast to known O-mannosylated proteins, single mannose residues (Man-α-Ser/Thr) are attached to this cell adhesion molecule. Conserved O-glycosylation sites in T-, E- and N-cadherins from different species, point to a general role of O-mannosyl glycans for cadherin function. |
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| Item Description: | Gesehen am 15.05.2017 |
| Physical Description: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2013.09.041 |