Truncated brush border myosin I affects membrane traffic in polarized epithelial cells
Truncated brush border myosin I affects membrane traffic in polarized epithelial cells
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DOI：
10.1034/j.1600-0854.2000.010506.x
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发表时间：
2000-05-01
期刊：
影响因子：
4.5
通讯作者：
Coudrier, E
中科院分区：
文献类型：
--
作者：
Durrbach, A;Raposo, G;Coudrier, E
在这项研究中，我们研究了肌动球蛋白驱动机制在极化细胞内吞作用中的潜在参与。我们观察到，使用 latrunculin A 解聚肌动蛋白丝会降低转铁蛋白再循环到 Caco-2 细胞基底外侧质膜的速率，并增加其向顶端质膜的递送。为了分析肌球蛋白是否参与内吞作用，我们在这种极化细胞系中产生了截短的、无功能的刷状缘肌球蛋白 I 蛋白 (BBMI)，我们之前已证明该蛋白对非极化细胞的内吞作用具有显着的负面影响。这些非功能性蛋白质影响转铁蛋白的再循环速率和二肽基肽酶 IV 从基底外侧质膜到顶端质膜的跨上皮转运速率。它们改变了顶端多囊泡内体中内化内吞示踪剂的分布，这些内吞示踪剂可被从顶端和基底外侧质膜域内化的液相示踪剂所接近。总而言之，这些观察结果表明，肌动球蛋白驱动的机制参与了基底外侧内化分子向顶端质膜的运输。
We investigate, in this study, the potential involvement of an acto-myosin-driven mechanism in endocytosis of polarized cells. We observed that depolymerization of actin filaments using latrunculin A decreases the rate of transferrin recycling to the basolateral plasma membrane of Caco-2 cells, and increases its delivery to the apical plasma membrane. To analyze whether a myosin was involved in endocytosis, we produced, in this polarized cell line, truncated, non-functional, brush border, myosin I proteins (BBMI) that we have previously demonstrated to have a dominant negative effect on endocytosis of unpolarized cells. These non-functional proteins affect the rate of transferrin recycling and the rate of transepithelial transport of dipeptidyl-peptidase IV from the basolateral plasma membrane to the apical plasma membrane. They modify the distribution of internalized endocytic tracers in apical multivesicular endosomes that are accessible to fluid phase tracers internalized from apical and basolateral plasma membrane domains. Altogether, these observations suggest that an acto-myosin-driven mechanism is involved in the trafficking of basolaterally internalized molecules to the apical plasma membrane.