Protein 4.1N is required for the formation of the lateral membrane domain in human bronchial epithelial cells.

Protein 4.1N is required for the formation of the lateral membrane domain in human bronchial epithelial cells.
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人支气管上皮细胞侧膜结构域的形成需要蛋白 4.1N

DOI:
10.1016/j.bbamem.2018.02.009
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发表时间:
2018-05
期刊:
Biochimica et biophysica acta. Biomembranes
影响因子:
--
通讯作者:
Chen L
Chen L
中科院分区:
其他
文献类型:
--
作者:
Wang Y;Zhang H;Kang Q;Liu J;Weng H;Li W;Mohandas N;An X;Chen L

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膜骨架在质膜的细胞质侧形成支架。红细胞膜代表了这种结构组织的原型。据文献记载,类似的膜骨架也存在于高尔基复合体中。先前已经表明,βII血影蛋白和锚蛋白G定位于人支气管上皮细胞的侧膜。在这里,我们发现蛋白4.1N也位于侧膜上,在那里它与E-钙粘蛋白,β-连环蛋白和βII血影蛋白结合。重要的是,在人支气管上皮细胞中通过RNAi耗尽4.1N导致侧膜高度降低,这在小鼠4.1N的重新表达后逆转。此外,尽管4. 1 N耗竭细胞的侧膜生物合成的初始阶段正常进行,但与对照细胞相比,4. 1 N耗竭细胞的侧膜的最终高度较短。我们的研究结果与以前的研究结果表明,4.1N,βII血影蛋白和锚蛋白G是侧膜骨架的结构组成部分,这种骨架在功能齐全的侧膜的组装中起着至关重要的作用。
The membrane skeleton forms a scaffold on the cytoplasmic side of the plasma membrane. The erythrocyte membrane represents an archetype of such structural organization. It has been documented that a similar membrane skeleton also exits in the Golgi complex. It has been previously shown that βII spectrin and ankyrin G are localized at the lateral membrane of human bronchial epithelial cells. Here we show that protein 4.1N is also located at the lateral membrane where it associates E-cadherin, β-catenin and βII spectrin. Importantly, depletion of 4.1N by RNAi in human bronchial epithelial cells resulted in decreased height of lateral membrane, which was reversed following re-expression of mouse 4.1N. Furthermore, although the initial phase of lateral membrane biogenesis proceeded normally in 4.1N-depleted cells, the final height of the lateral membrane of 4.1N-depleted cells was shorter compared to that of control cells. Our findings together with previous findings imply that 4.1N, βII spectrin and ankyrin G are structural components of the lateral membrane skeleton and that this skeleton plays an essential role in the assembly of a fully functional lateral membrane.
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