Distinct roles of Rab3B and Rab13 in the polarized transport of apical, basolateral, and tight junctional membrane proteins to the plasma membrane
| Autor: | Yasuyo Yamamoto, Shinya Morimoto, Hiro-omi Kanayama, Shinji Manabe, Noriyuki Nishimura, Susumu Kagawa, Takuya Sasaki, Hiroko Kitamura |
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| Rok vydání: | 2003 |
| Předmět: |
rab3 GTP-Binding Proteins
Biophysics Biological Transport Active Receptors Nerve Growth Factor Biology In Vitro Techniques Biochemistry Receptor Nerve Growth Factor Cell Line Tight Junctions Mice Cricetinae Cell polarity Claudin-1 Animals Humans Claudin Molecular Biology Epithelial polarity Tight junction Cell Membrane Cell Polarity Membrane Proteins Cell Biology Membrane transport Recombinant Proteins Cell biology Vesicular transport protein Membrane protein Receptors LDL rab GTP-Binding Proteins Mutagenesis Site-Directed Cattle Rab Caco-2 Cells HeLa Cells trans-Golgi Network |
| Zdroj: | Biochemical and biophysical research communications. 308(2) |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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