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FEBS Lett. 2013 Nov 15;587(22):3715-21. doi: 10.1016/j.febslet.2013.09.041. Epub 2013 Oct 7.

O-glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues.

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Centre for Organismal Studies Heidelberg, University of Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany; Center for Molecular Biology, University of Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.


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.


CDH13; CID; ConA; EC; ER; GPI; Glycosylation; H-cadherin; LC–MS; Mass spectrometry; O-mannosylation; POMT; T-cad; T-cadherin; XIC; collision-induced dissociation; concanavalin A; endoplasmic reticulum; extracellular cadherin; extracted ion chromatogram; glycosylphosphatidylinositol; liquid chromatography–mass spectrometry; protein O-mannosyltransferase; α-DG; α-dystroglycan

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