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dc.contributor.authorGrayson, Cen_US
dc.contributor.authorBartolini, Fen_US
dc.contributor.authorChapple, JPen_US
dc.contributor.authorWillison, KRen_US
dc.contributor.authorBhamidipati, Aen_US
dc.contributor.authorLewis, SAen_US
dc.contributor.authorLuthert, PJen_US
dc.contributor.authorHardcastle, AJen_US
dc.contributor.authorCowan, NJen_US
dc.contributor.authorCheetham, MEen_US
dc.identifier.citationHUMAN MOLECULAR GENETICS, 2002, 11 pp. 3065 - 3074en_US
dc.description.abstractMutations in the retinitis pigmentosa 2 (RP2) gene cause a severe form of X-linked retinal degeneration. RP2 is a ubiquitous 350 amino acid plasma membrane-associated protein, which shares homology with the tubulin-specific chaperone cofactor C. RP2 protein, like cofactor C, stimulates the GTPase activity of tubulin in combination with cofactor D. RP2 has also been shown to interact with ADP ribosylation factor-like 3 (Arl3) in a nucleotide and myristoylation-dependant manner. In this study we have examined the relationship between RP2, cofactor C and Arl3 in patient-derived cell lines and in the retina. Examination of lymphoblastoid cells from patients with an Arg120stop nonsense mutation in RP2 revealed that the expression levels of cofactor C and Arl3 were not affected by the absence of RP2. In human retina, RP2 was localized to the plasma membrane of cells throughout the retina. RP2 was present at the plasma membrane in both rod and cone photoreceptors, extending from the outer segment through the inner segment to the synaptic terminals. There was no enrichment of RP2 staining in any photoreceptor organelle. In contrast, cofactor C and Arl3 localized predominantly to the photoreceptor connecting cilium in rod and cone photoreceptors. Cofactor C was cytoplasmic in distribution, whereas Arl3 localized to other microtubule structures within all cells. Arl3 behaved as a microtubule-associated protein: it co-localized with microtubules in HeLa cells and this was enhanced following microtubule stabilization with taxol. Furthermore, Arl3 co-purified with microtubules from bovine brain. Following microtubule depolymerization with nocodazole, Arl3 relocalized to the nuclear membrane. These data suggest that RP2 functions in concert with Arl3 to link the cell membrane with the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery.en_US
dc.format.extent3065 - 3074en_US
dc.titleLocalization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3en_US
dc.typeJournal Article
rioxxterms.typeJournal Article/Reviewen_US
pubs.notesresearcherid-numbers: Cheetham, Michael/B-4672-2011 orcid-numbers: Luthert, Philip/0000-0001-7276-6898 Cheetham, Michael/0000-0001-6429-654X unique-id: ISI:000179120100008en_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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