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首页> 外文期刊>Journal of Cellular Physiology >Identification and characterization of site‐specific N‐glycosylation in the potassium channel Kv3.1b
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Identification and characterization of site‐specific N‐glycosylation in the potassium channel Kv3.1b

机译:识别和描述地理地理位置特殊的N糖基化钾通道Kv3.1b

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The potassium ion channel Kv3.1b is a member of a family of voltage‐gated ion channels that are glycosylated in their mature form. In the present study, we demonstrate the impact of N‐glycosylation at specific asparagine residues on the trafficking of the Kv3.1b protein. Large quantities of asparagine 229 (N229)‐glycosylated Kv3.1b reached the plasma membrane, whereas N220‐glycosylated and unglycosylated Kv3.1b were mainly retained in the endoplasmic reticulum (ER). These ER‐retained Kv3.1b proteins were susceptible to degradation, when co‐expressed with calnexin, whereas Kv3.1b pools located at the plasma membrane were resistant. Mass spectrometry analysis revealed a complex type Hex 3 HexNAc 4 Fuc 1 glycan as the major glycan component of the N229‐glycosylated Kv3.1b protein, as opposed to a high‐mannose type Man 8 GlcNAc 2 glycan for N220‐glycosylated Kv3.1b. Taken together, these results suggest that trafficking‐dependent roles of the Kv3.1b potassium channel are dependent on N229 site‐specific glycosylation and N‐glycan structure, and operate through a mechanism whereby specific N‐glycan structures regulate cell surface expression.
机译:钾离子通道Kv3.1b的一员家庭的电压检测封闭的离子通道糖基化的成熟的形式。研究中,我们展示的影响在特定的天冬酰胺残留地理N糖基化贩卖的Kv3.1b蛋白质。大量的天冬酰胺229 (N229)糖化Kv3.1b到达等离子体膜,而N220糖化和unglycosylated Kv3.1b主要保留在内质网(ER)。容易降解,当公司表示与calnexin,而Kv3.1b池位于质膜耐药。谱分析揭示了一个复杂类型十六进制3 HexNAc 4 Fuc 1多糖为最主要的多糖N229糖化Kv3.1b应承担的组件蛋白质,而不是高甘露糖型8人GlcNAc 2多糖N220糖化Kv3.1b。总的来说,这些结果表明,贩卖量依赖Kv3.1b的角色钾离子通道是依赖N229地理位置特定的糖基化和N的多糖结构和运行机制即特定N多糖结构调节细胞表面表达。

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