![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on April 1, 2004
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on August 29, 2003
Revised on December 11, 2003
Accepted on December 31, 2003
-catenin
1 Child Health Research Institute, North Adelaide, SA 5006, Australia; Centre for the Molecular Genetics of Development, University of Adelaide, SA 5005, Australia
2 Child Health Research Institute, North Adelaide, SA 5006, Australia
* Corresponding author. E-mail address: stephen.wood{at}adelaide.edu au.
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, 
-catenin. Here we show, in the polarised intestinal epithelial cell line T84, FAM localized to multiple points of protein trafficking. FAM interacted with -catenin and E-cadherin in T84 cells but only in subconfluent cultures. FAM extensively colocalized with -catenin in cytoplasmic puncta but not at sites of cell-cell contact as well as immunoprecipitating with -catenin and E-cadherin from a higher molecular weight complex (approximately 500 kDa). At confluence FAM neither colocalized with, nor immunoprecipitated, -catenin or E-cadherin which were predominantly in a larger molecular weight complex (approximately 2MDa) at the cell surface. Overexpression of FAM in MCF-7 epithelial cells resulted in increased -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 -catenin during trafficking to the plasma membrane.
This article has been cited by other articles:
|
|
 |
|
  R. Mouchantaf, B. A. Azakir, P. S. McPherson, S. M. Millard, S. A. Wood, and A. Angers The Ubiquitin Ligase Itch Is Auto-ubiquitylated in Vivo and in Vitro but Is Protected from Degradation by Interacting with the Deubiquitylating Enzyme FAM/USP9X J. Biol. Chem., December 15, 2006; 281(50): 38738 - 38747. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Amerik, N. Sindhi, and M. Hochstrasser A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function J. Cell Biol., December 4, 2006; 175(5): 825 - 835. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Van Hoof, R. Passier, D. Ward-Van Oostwaard, M. W. H. Pinkse, A. J. R. Heck, C. L. Mummery, and J. Krijgsveld A Quest for Human and Mouse Embryonic Stem Cell-specific Proteins Mol. Cell. Proteomics, July 1, 2006; 5(7): 1261 - 1273. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. M. Millard and S. A. Wood Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes J. Cell Biol., May 22, 2006; 173(4): 463 - 468. [Abstract] [Full Text] [PDF]
|
|
