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- W2895529681 abstract "Impairment of Kv1.3 membrane expression in leukocytes and sensory neuron contributes to the pathophysiology of autoimmune diseases and sensory syndromes. Molecular mechanisms underlying Kv1.3 channel trafficking to the plasma membrane remain elusive. We report a novel non-canonical di-acidic signal (E483/484) at the C-terminus of Kv1.3 essential for anterograde transport and surface expression. Notably, homologous motifs are conserved in neuronal Kv1 and Shaker channels. Biochemical analysis reveals interactions with the Sec24 subunit of the coat protein complex II. Disruption of this complex drastically retains the channel at the endoplasmic reticulum. A molecular model of the Kv1.3-Sec24a complex suggests salt-bridges between the di-acidic E483/484 motif in Kv1.3 and the di-basic R750/752 sequence in Sec24. These findings identify a novel and previously unrecognized motif of Kv channels essential for their expression in the cell surface. Our results contribute to our understanding of how Kv1 channels target to the cell membrane, and provide new therapeutic strategies for the treatment of pathological conditions." @default.
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- W2895529681 date "2013-01-01" @default.
- W2895529681 modified "2023-10-17" @default.
- W2895529681 title "A non-canonical di-acidic signal at the C-terminal of Kv1.3 determines anterograde trafficking and surface expression" @default.
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- W2895529681 doi "https://doi.org/10.1242/jcs.134825" @default.
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