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dc.contributor.authorSullivan, A
dc.contributor.authorUff, CR
dc.contributor.authorIsacke, CM
dc.contributor.authorThorne, RF
dc.date.accessioned2018-06-11T14:32:48Z
dc.date.issued2003-04
dc.identifier.citationExperimental cell research, 2003, 284 (2), pp. 224 - 238
dc.identifier.issn0014-4827
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/1832
dc.identifier.eissn1090-2422
dc.identifier.doi10.1016/s0014-4827(02)00054-x
dc.description.abstractThe ERM proteins (ezrin, radixin, moesin) together with merlin comprise a subgroup of the band 4.1 superfamily. These proteins act as membrane cytoskeletal linker proteins mediating interactions between the cytoplasmic domains of transmembrane proteins and actin. To better understand how the ERM proteins function to regulate these junctional complexes, a yeast 2-hybrid screen was undertaken using ezrin as a bait. We describe here the identification and cloning of a novel protein, PACE-1, which binds to the C-terminal domain of ezrin. Characterization of PACE-1 in human breast cancer cell lines demonstrates it to have two distinct intracellular localizations. A proportion of the protein is associated with the cytoplasmic face of the Golgi apparatus. This distribution is dependent upon the presence of the PACE-1 N-terminal myristoylation consensus sequence but is not dependent on an association with ezrin. In contrast, PACE-1 colocalises with ezrin in the lamellipodia, where ezrin has a role in cell spreading and motility. A notable feature of PACE-1 is the presence of a putative N-terminal kinase domain; however, in biochemical assays PACE-1 was shown to have associated rather than intrinsic kinase activity. Together these data suggest that PACE-1 may play a role in regulating cell adhesion/migration complexes in migrating cells.
dc.formatPrint
dc.format.extent224 - 238
dc.languageeng
dc.language.isoeng
dc.subjectCOS Cells
dc.subjectTumor Cells, Cultured
dc.subjectCell Membrane
dc.subjectPseudopodia
dc.subjectGolgi Apparatus
dc.subjectEukaryotic Cells
dc.subjectAnimals
dc.subjectHumans
dc.subjectFatty Acids, Monounsaturated
dc.subjectCytoskeletal Proteins
dc.subjectPhosphoproteins
dc.subjectDNA, Complementary
dc.subjectCloning, Molecular
dc.subjectCell Adhesion
dc.subjectCell Movement
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectProtein Structure, Tertiary
dc.subjectProtein Binding
dc.subjectMolecular Sequence Data
dc.titlePACE-1, a novel protein that interacts with the C-terminal domain of ezrin.
dc.typeJournal Article
rioxxterms.versionofrecord10.1016/s0014-4827(02)00054-x
rioxxterms.licenseref.startdate2003-04
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfExperimental cell research
pubs.issue2
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research/Molecular Cell Biology
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Breast Cancer Research/Molecular Cell Biology
pubs.publication-statusPublished
pubs.volume284
pubs.embargo.termsNot known
icr.researchteamMolecular Cell Biologyen_US
dc.contributor.icrauthorIsacke, Clare


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