ArticleiScience2025
N-glycosylation modulates the inactivation kinetics of the Kv3.4 ion channel.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
In our previous study, when mapping the kinetics of all 40 genetic subtypes of the voltage-gated potassium (Kv) family of ion channels, we observed significant heterogeneity in the inactivation delay of Kv3.4. Kv3.4 enables high-frequency firing in excitable cells and is linked to disorders such as Alzheimer's disease, epilepsy, chronic pain, and cardiovascular disease. In this study, we found that N-glycosylation, a co- and post-translational process of adding glycans branches to proteins, is a key mechanism that causes heterogeneity in the inactivation delay of Kv3.4 ion channel. Additionally, we discovered that changes in glucose availability directly affect N-glycosylation and the kinetics of Kv3.4, along with other N-glycosylated Kvs, making glucose a key regulator of Kv activity and, consequently, cell excitability. We propose that disruptions in N-glycosylation of Kv3.4 ion channels may play a role in neurological disorders linked to impaired glucose metabolism.
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