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O ‐glycosylation of the non‐canonical T‐cadherin from rabbit skeletal muscle by single mannose residues
Author(s) -
Winterhalter Patrick R.,
Lommel Mark,
Ruppert Thomas,
Strahl Sabine
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.041
Subject(s) - glycosylation , mannose , glycan , cadherin , glycoprotein , chemistry , biochemistry , microbiology and biotechnology , biology , cell
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.