The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and β-catenin

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dc.contributor.authorMurray, R.
dc.contributor.authorJolly, L.
dc.contributor.authorWood, S.
dc.contributor.organisationCentre for the Molecular Genetics of Development
dc.date.issued2004
dc.descriptionCopyright © 2004 by The American Society for Cell Biology.
dc.description.abstractUbiquitylation 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.
dc.description.statementofresponsibilityRachael Z. Murray, Lachlan A. Jolly and Stephen A. Wood
dc.identifier.citationMolecular Biology of the Cell, 2004; 15(4):1591-1599
dc.identifier.doi10.1091/mbc.E03-08-0630
dc.identifier.issn1059-1524
dc.identifier.issn1939-4586
dc.identifier.orcidJolly, L. [0000-0003-4538-2658]
dc.identifier.urihttp://hdl.handle.net/2440/3113
dc.language.isoen
dc.publisherAmer Soc Cell Biology
dc.source.urihttps://doi.org/10.1091/mbc.e03-08-0630
dc.subjectEpithelium
dc.subjectCell Line
dc.subjectCell Line, Tumor
dc.subjectCell Membrane
dc.subjectCytoplasm
dc.subjectGolgi Apparatus
dc.subjectFibroblasts
dc.subjectHumans
dc.subjectMyosins
dc.subjectUbiquitin Thiolesterase
dc.subjectEndopeptidases
dc.subjectActinin
dc.subjectCytoskeletal Proteins
dc.subjectTrans-Activators
dc.subjectCadherins
dc.subjectUbiquitin
dc.subjectDetergents
dc.subjectMicroscopy, Fluorescence
dc.subjectPrecipitin Tests
dc.subjectChromatography, Gel
dc.subjectTransfection
dc.subjectCell Adhesion
dc.subjectProtein Transport
dc.subjectPlasmids
dc.subjectbeta Catenin
dc.subjectMass Spectrometry
dc.titleThe FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and β-catenin
dc.title.alternativeThe FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and beta-catenin
dc.typeJournal article
pubs.publication-statusPublished

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