Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/3113
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Type: | Journal article |
Title: | The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and β-catenin |
Other Titles: | The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and beta-catenin |
Author: | Murray, R. Jolly, L. Wood, S. |
Citation: | Molecular Biology of the Cell, 2004; 15(4):1591-1599 |
Publisher: | Amer Soc Cell Biology |
Issue Date: | 2004 |
ISSN: | 1059-1524 1939-4586 |
Organisation: | Centre for the Molecular Genetics of Development |
Statement of Responsibility: | Rachael Z. Murray, Lachlan A. Jolly and Stephen A. Wood |
Abstract: | Ubiquitylation is a necessary step in the endocytosis and lysosomal trafficking of many plasma membrane proteins and can also influence protein trafficking in the biosynthetic pathway. Although a molecular understanding of ubiquitylation in these processes is beginning to emerge, very little is known about the role deubiquitylation may play. Fat Facets in mouse (FAM) is substrate-specific deubiquitylating enzyme highly expressed in epithelia where it interacts with its substrate, β-catenin. Here we show, in the polarized intestinal epithelial cell line T84, FAM localized to multiple points of protein trafficking. FAM interacted with β-catenin and E-cadherin in T84 cells but only in subconfluent cultures. FAM extensively colocalized with β-catenin in cytoplasmic puncta but not at sites of cell-cell contact as well as immunoprecipitating with β-catenin and E-cadherin from a higher molecular weight complex (500 kDa). At confluence FAM neither colocalized with, nor immunoprecipitated, β-catenin or E-cadherin, which were predominantly in a larger molecular weight complex (2 MDa) at the cell surface. Overexpression of FAM in MCF-7 epithelial cells resulted in increased β-catenin levels, which localized to the plasma membrane. Expression of E-cadherin in L-cell fibroblasts resulted in the relocalization of FAM from the Golgi to cytoplasmic puncta. These data strongly suggest that FAM associates with E-cadherin and β-catenin during trafficking to the plasma membrane. |
Keywords: | Epithelium Cell Line Cell Line, Tumor Cell Membrane Cytoplasm Golgi Apparatus Fibroblasts Humans Myosins Ubiquitin Thiolesterase Endopeptidases Actinin Cytoskeletal Proteins Trans-Activators Cadherins Ubiquitin Detergents Microscopy, Fluorescence Precipitin Tests Chromatography, Gel Transfection Cell Adhesion Protein Transport Plasmids beta Catenin Mass Spectrometry |
Description: | Copyright © 2004 by The American Society for Cell Biology. |
DOI: | 10.1091/mbc.E03-08-0630 |
Published version: | http://dx.doi.org/10.1091/mbc.e03-08-0630 |
Appears in Collections: | Aurora harvest 6 Centre for the Molecular Genetics of Development publications Molecular and Biomedical Science publications |
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