Distinct roles of Rab3B and Rab13 in the polarized transport of apical, basolateral, and tight junctional membrane proteins to the plasma membrane
Distinct roles of Rab3B and Rab13 in the polarized transport of apical, basolateral, and tight junctional membrane proteins to the plasma membrane
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DOI：
10.1016/s0006-291x(03)01358-5
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发表时间：
2003-08-22
影响因子：
3.1
通讯作者：
Sasaki, T
中科院分区：
文献类型：
--
作者：
Yamamoto, Y;Nishimura, N;Sasaki, T
在所有真核细胞中，蛋白质向不同质膜结构域的调节转运对于细胞极性的建立和维持是必不可少的。Rab家族小G蛋白在决定囊泡转运途径的特异性方面起着至关重要的作用。Rab 3B和Rab 13定位于极化上皮细胞的紧密连接和非极化成纤维细胞的胞质泡状结构，但其功能知之甚少。在这里，我们研究了他们的作用，在调节顶端p75神经营养因子受体（p75 NTR），基底外侧低密度脂蛋白受体（LDLR），紧密连接Claudin-1的细胞表面转运使用非极化成纤维细胞的运输试验。Rab 3B突变体的过表达抑制LDLR的细胞表面转运，但不抑制p75 NTR和Claudin-1。相反，Rab 13突变体的过度表达损害了Claudin-1的转运，但不损害LDLR和p75 NTR。这些结果表明Rab 3B和Rab 13分别指导LDLR和Claudin-1的细胞表面转运，并可能有助于上皮极化。(C)2003年爱思唯尔公司All rights reserved.
Regulated transport of proteins to distinct plasma membrane domains is essential for the establishment and maintenance of cell polarity in all eukaryotic cells. The Rab family small G proteins play a crucial role in determining the specificity of vesicular transport pathways. Rab3B and Rab13 localize to tight junction in polarized epithelial cells and cytoplasmic vesicular structures in non-polarized fibroblasts, but their functions are poorly understood. Here we examined their roles in regulating the cell-surface transport of apical p75 neurotrophin receptor (p75NTR), basolateral low-density lipoprotein receptor (LDLR), and tight junctional Claudin-1 using transport assay in non-polarized fibroblasts. Overexpression of Rab3B mutants inhibited the cell-surface transport of LDLR, but not p75NTR and Claudin-1. In contrast, overexpression of Rab13 mutants impaired the transport of Claudin-1, but not LDLR and p75NTR. These results suggest that Rab3B And Rab13 direct the cell-surface transport of LDLR and Claudin-1, respectively, and may contribute to epithelial polarization. (C) 2003 Elsevier Inc. All rights reserved.