Vangl2 regulates E-cadherin in epithelial cells.
E-cadherin belongs to the classic cadherin subfamily of calcium-dependent cell adhesion molecules and is crucial for the formation and function of epithelial adherens junctions. In this study, we demonstrate that Vangl2, a vertebrate regulator of planar cell polarity (PCP), controls E-cadherin in epithelial cells. E-cadherin co-immunoprecipitates with Vangl2 from embryonic kidney extracts, and this association is also observed in transfected fibroblasts. Vangl2 enhances the internalization of E-cadherin when overexpressed. Conversely, the quantitative ratio of E-cadherin exposed to the cell surface is increased in cultured renal epithelial cells derived from Vangl2(Lpt/+) mutant mice. Interestingly, Vangl2 is also internalized through protein traffic involving Rab5- and Dynamin-dependent endocytosis. Taken together with recent reports regarding the transport of Frizzled3, MMP14 and nephrin, these results suggest that one of the molecular functions of Vangl2 is to enhance the internalization of specific plasma membrane proteins with broad selectivity. This function may be involved in the control of intercellular PCP signalling or in the PCP-related rearrangement of cell adhesions.
Laboratory of Molecular Neuroimaging, Graduate School of Medical and Dental Sciences, Niigata University, Niigata, Niigata 951-8510, Japan.
Tadahiro
T
Nagaoka
Department of Neuroscience II, Research Institute of Environmental Medicine, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Ayumu
A
Inutsuka
Department of Microbiology and Hygiene, Bangladesh Agricultural University, Mymensingh 2202. Bangladesh.
Khadiza
K
Begum
Department of Microbiology and Hygiene, Bangladesh Agricultural University, Mymensingh 2202. Bangladesh.
Khandakar musabbir
Km
Bin hafiz
Laboratory of Molecular Neuroimaging, Graduate School of Medical and Dental Sciences, Niigata University, Niigata, Niigata 951-8510, Japan.
Masashi
M
Kishi
D022005:Adherens Junctions / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D015820:Cadherins / Q000235:genetics* / Q000378:metabolism; D002448:Cell Adhesion; D002452:Cell Count; D002462:Cell Membrane / Q000378:metabolism*; D016764:Cell Polarity; D034281:Dynamins / Q000235:genetics / Q000378:metabolism; D004622:Embryo, Mammalian; D004705:Endocytosis; D004847:Epithelial Cells / Q000378:metabolism* / Q000648:ultrastructure; D005347:Fibroblasts / Q000378:metabolism / Q000648:ultrastructure; D005786:Gene Expression Regulation; D007668:Kidney / Q000166:cytology / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D008822:Mice, Transgenic; D009419:Nerve Tissue Proteins / Q000235:genetics* / Q000378:metabolism; D021381:Protein Transport; D015398:Signal Transduction; D020696:rab5 GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism
D015820:Cadherins; C431577:Ltap protein, mouse; D009419:Nerve Tissue Proteins; D020696:rab5 GTP-Binding Proteins; D034281:Dynamins