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

• Verfasst von: Winterhalter, Patrick R. [VerfasserIn]
• Verfasst von: Lommel, Mark [VerfasserIn]
• Verfasst von: Ruppert, Thomas [VerfasserIn]
• Verfasst von: Strahl, Sabine [VerfasserIn]
• Titel: O-glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues
• Verf.angabe: Patrick R. Winterhalter, Mark Lommel, Thomas Ruppert, Sabine Strahl
• Umfang: 7 S.
• Fussnoten: Gesehen am 15.05.2017
• Titel Quelle: Enthalten in: Vereinigung der Europäischen Biochemischen Gesellschaften: FEBS letters
• Jahr Quelle: 2013
• Band/Heft Quelle: 587(2013), 22, S. 3715-3721
• ISSN Quelle: 1873-3468
• DOI: doi:10.1016/j.febslet.2013.09.041
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1558584560

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.