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MAL蛋白在Madin-Darby犬肾细胞的顶端表面调节网格蛋白介导的内吞作用。

MAL regulates clathrin-mediated endocytosis at the apical surface of Madin-Darby canine kidney cells.

作者信息

Martín-Belmonte Fernando, Martínez-Menárguez José A, Aranda Juan F, Ballesta José, de Marco María C, Alonso Miguel A

机构信息

Centro de Biología Molecular "Severo Ochoa", Universidad Autónoma de Madrid and Consejo Superior de Investigaciones Científicas, Cantoblanco, Madrid, 28049 Spain.

出版信息

J Cell Biol. 2003 Oct 13;163(1):155-64. doi: 10.1083/jcb.200304053. Epub 2003 Oct 6.

DOI:10.1083/jcb.200304053
PMID:14530381
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2173443/
Abstract

MAL is an integral protein component of the machinery for apical transport in epithelial Madin-Darby canine kidney (MDCK) cells. To maintain its distribution, MAL cycles continuously between the plasma membrane and the Golgi complex. The clathrin-mediated route for apical internalization is known to differ from that at the basolateral surface. Herein, we report that MAL depends on the clathrin pathway for apical internalization. Apically internalized polymeric Ig receptor (pIgR), which uses clathrin for endocytosis, colocalized with internalized MAL in the same apical vesicles. Time-lapse confocal microscopic analysis revealed cotransport of pIgR and MAL in the same endocytic structures. Immunoelectron microscopic analysis evidenced colabeling of MAL with apically labeled pIgR in pits and clathrin-coated vesicles. Apical internalization of pIgR was abrogated in cells with reduced levels of MAL, whereas this did not occur either with its basolateral entry or the apical internalization of glycosylphosphatidylinositol-anchored proteins, which does not involve clathrin. Therefore, MAL is critical for efficient clathrin-mediated endocytosis at the apical surface in MDCK cells.

摘要

MAL是上皮性犬肾（MDCK）细胞顶端运输机制的一种整合蛋白成分。为维持其分布，MAL在质膜和高尔基体复合体之间持续循环。已知网格蛋白介导的顶端内化途径与基底外侧表面的不同。在此，我们报告MAL顶端内化依赖于网格蛋白途径。顶端内化的聚合免疫球蛋白受体（pIgR）利用网格蛋白进行内吞作用，它与内化的MAL在相同的顶端囊泡中共定位。延时共聚焦显微镜分析显示pIgR和MAL在相同的内吞结构中共转运。免疫电子显微镜分析证明MAL与顶端标记的pIgR在小窝和网格蛋白包被小泡中共同标记。在MAL水平降低的细胞中，pIgR的顶端内化被消除，而其基底外侧内吞或糖基磷脂酰肌醇锚定蛋白的顶端内化（不涉及网格蛋白）则未发生这种情况。因此，MAL对于MDCK细胞顶端表面高效的网格蛋白介导的内吞作用至关重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/a5415829e55e/200304053f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/2c36ec09917a/200304053f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/f14fa69ec9b5/200304053f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/1e8048e6cf10/200304053f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/74278877a83a/200304053f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/f34f9ebb5a8d/200304053f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/a5415829e55e/200304053f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/2c36ec09917a/200304053f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/f14fa69ec9b5/200304053f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/1e8048e6cf10/200304053f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/74278877a83a/200304053f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/f34f9ebb5a8d/200304053f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f57a/2173443/a5415829e55e/200304053f6.jpg

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