A hyperglycosylated form of Kv 1.2 upregulated in LGI1 knockout mice
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Kv 1 voltage-gated potassium channels determine key functional neuronal properties. Their activity is modulated by subunit composition and post-translational modifications such as phosphorylation and glycosylation. Using an antibody directed against a phosphotyrosine (Y 458 ) located in the C-terminal tail of Kv 1.2 , we identified yet unreported high molecular weight forms of Kv 1.2 among them, a phosphorylated and heavily glycosylated 100 kDa form. Owing to the significant downregulation of Kv 1.2 in LGI1-dependent autosomal dominant lateral temporal lobe epilepsy, we investigated, in total brain and the hippocampal formation of both WT and Lgi1 -/- mice, the distribution of phosphoY 458 Kv 1.2 and we compared their respective proteomic interactomes with those of Kv 1.2 . In addition to major differences between the interactomes of pY 458 Kv 1.2 and Kv 1.2 in WT and Lgi1 -/- , we found a major reshaping of pY 458 Kv 1.2 molecular neighbourhood between WT and Lgi1 -/- as well as a significant upregulation of the glycosylated form in Lgi1 -/- .
