O-glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues |
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Authors: | Patrick R Winterhalter Mark Lommel Thomas Ruppert Sabine Strahl |
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Institution: | 1. Centre for Organismal Studies Heidelberg, University of Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany;2. Center for Molecular Biology, University of Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany |
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Abstract: | 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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Keywords: | T-cad T-cadherin CID collision-induced dissociation ConA concanavalin A α-DG α-dystroglycan EC extracellular cadherin ER endoplasmic reticulum GPI glycosylphosphatidylinositol LC&ndash MS liquid chromatography&ndash mass spectrometry POMT protein O-mannosyltransferase XIC extracted ion chromatogram |
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