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dc.contributor.authorChapple, JPen_US
dc.contributor.authorGrayson, Cen_US
dc.contributor.authorHardcastle, AJen_US
dc.contributor.authorBailey, TAen_US
dc.contributor.authorMatter, Ken_US
dc.contributor.authorAdamson, Pen_US
dc.contributor.authorGraham, CHen_US
dc.contributor.authorWillison, KRen_US
dc.contributor.authorCheetham, MEen_US
dc.identifier.citationBIOCHEMICAL JOURNAL, 2003, 372 pp. 427 - 433en_US
dc.description.abstractMutations in the retinitis pigmentosa protein gene RP2 account for up to 15 % of X-linked retinitis pigmentosa. RP2 is a novel protein of unknown function, which is targeted to the plasma membrane by dual N-terminal acyl-modification. Dual-acylated proteins are targeted to lipid rafts, and some are subject to polarized sorting. Therefore we investigated the organization of RP2 on the plasma membrane. Endogenous RP2 protein was predominantly localized at the plasma membrane, and exogenously expressed green-fluorescent-protein-tagged protein was also targeted to the membrane in a wide range of cultured cells. High levels of endogenous RP2 protein were present in HeLa cells and in the retinal pigment epithelium-derived cell line ARPE19. A significant proportion of RP2 in cultured neuroblastoma cells was associated with detergent-resistant membranes (DRMs), but much less than other dually acylated proteins (e.g. Lyn and Fyn). In contrast, the RP2-interacting protein Arl3 (ADP-ribosylation factor-like 3) was not found to be associated with DRMs. The association of RP2 with DRMs was cholesterol-dependent. In polarized epithelial cells in culture and in vivo, RP2 was present in both the apical and basolateral domains of the plasma membrane. These data show that RP2 is not specific to either domain, unlike some other dually acylated proteins. Interestingly, the level of RP2 protein increased in the epithelial cell line Caco-2 with differentiation and polarization. These data show that RP2 is present on the membrane of all cell types examined both in vitro and in vivo, and that RP2 associates with lipid rafts, suggesting a potential role for the protein in signal transduction.en_US
dc.format.extent427 - 433en_US
dc.titleOrganization on the plasma membrane of the retinitis pigmentosa protein RP2: investigation of association with detergent-resistant membranes and polarized sortingen_US
dc.typeJournal Article
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfBIOCHEMICAL JOURNALen_US
pubs.notesaffiliation: Cheetham, ME (Reprint Author), UCL, Inst Ophthalmol, Div Pathol, London WC1E 6BT, England. UCL, Inst Ophthalmol, Div Pathol, London WC1E 6BT, England. UCL, Inst Ophthalmol, Div Mol Genet, London, England. UCL, Inst Ophthalmol, Div Cell Biol, London, England. GKT Med & Dent Sch, Mol Neurobiol Grp, London, England. Inst Canc Res, Chester Beatty Labs, London SW3 6JB, England. keywords: dual acylation; lipid raft; protein targeting; retinal degeneration; tubulin-folding cofactor keywords-plus: CANINE KIDNEY-CELLS; TYROSINE KINASE; EPITHELIAL-CELLS; TIGHT JUNCTION; COFACTOR-C; PALMITOYLATION; LOCALIZATION; MICRODOMAINS; MUTATIONS; RAFTS research-areas: Biochemistry & Molecular Biology web-of-science-categories: Biochemistry & Molecular Biology author-email: researcherid-numbers: Matter, Karl/C-4880-2008 Cheetham, Michael/B-4672-2011 orcid-numbers: Matter, Karl/0000-0001-8026-7220 Chapple, Paul/0000-0003-1876-1505 Cheetham, Michael/0000-0001-6429-654X number-of-cited-references: 41 times-cited: 19 usage-count-last-180-days: 0 usage-count-since-2013: 1 journal-iso: Biochem. J. doc-delivery-number: 691VD unique-id: ISI:000183625800015 oa: gold_or_bronze da: 2018-09-12en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Chromatin Regulation
pubs.embargo.termsNot knownen_US
icr.researchteamChromatin Regulationen_US
dc.contributor.icrauthorWillison, Keithen_US

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