Positional cloning of the gene for X-linked retinitis pigmentosa 2

Schwahn, Uwe; Lenzner, Steffen; Dong, Juan; Feil, Silke; Hinzmann, Bernd; Duijnhoven, G.C.F. van; Kirschner, Renate; Hemberger, Myriam; Bergen, Arthur A. B.; Rosenberg, Thomas; Pinckers, A.; Fundele, Reinald; Rosenthal, André; Cremers, Frans P.M.; Ropers, Hans‐Hilger; Berger, Wolfgang

doi:10.1038/1214

Cited by 334 publications

(282 citation statements)

References 33 publications

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“…They are important for the maintenance of photoreceptor cells, since knockouts of Arl3 or HRG4 cause strong retinal defects in mice and mutations of RP2 are causing retinitis pigmentosa [18,19,30]. The Arl3 À/À deletion mice exhibit a mislocalization of rhodopsin and probably also other proteins that are important for phototransduction.…”

Section: Discussionmentioning

confidence: 99%

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Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

et al. 2008

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Arl2 and Arl3, members of the Arf subfamily of small G proteins, are believed to be involved in ciliary and microtubuledependent processes. Recently, we could identify RP2, responsible for a variant of X-linked retinitis pigmentosa, as the Arl3-specific GAP. Here, we have characterized Arl2/3 interactions. We show the formation of a ternary complex between Arl3, its cognate GAP RP2 and its retinal effector HRG4. This complex seems to be important for photoreceptor function.

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Section: Discussionmentioning

confidence: 99%

“…We have shown that the proposed Arl3 effector RP2 is actually a highly efficient and specific Arl3GAP with only limited activity on Arl2 [9]. RP2 is a protein mutated in patients with X-linked retinitis pigmentosa 2 [19] and displays sequence and functional homology to CoC.…”

Section: Introductionmentioning

confidence: 99%

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

et al. 2008

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“…On the basis of linkage analyses, the frequency of RP3 as a fraction of XLRP is 56 to 90%, and RP2 accounts for most of the remainder Ott et al, 1990;Teague et al, 1994;Bergen et al, 1995;Fujita et al, 1997]. Cloning of RP2 in Xp11.23 [Schwahn et al, 1998] (MIM# 312600) and subsequent mutation analysis have confirmed that RP2 accounts for 10 to 25% of XLRP. Two other XLRP loci have been mapped in single pedigrees: RP23 at Xp22 (GDB# 9837371) and RP24 at Xq26-27 [Gieser et al, 1998] (MIM# 300155).…”

Section: Introductionmentioning

confidence: 99%

Mutations ofRPGR in X-linked retinitis pigmentosa (RP3)

Vervoort

Wright

2002

Hum. Mutat.

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Mutations in RPGR, retinitis pigmentosa GTPase regulator, are associated with RP3 type of Xlinked retinitis pigmentosa, a severe, non-syndromic form of retinal degeneration. In the majority of subjects RPGR mutations are associated with a typical rod-cone degeneration, but in a small number, cone-rod dystrophy, deafness, and abnormalities in respiratory cilia have been noted. Alternative splicing of RPGR is complex in all species examined. In RP3 patients, mutations have been found in exons 1 14 and ORF15, thus delineating a transcript necessary for normal retinal function in humans. The great majority of mutations are predicted to result in premature termination of translation. These mutations are scattered over exons 1 14 and ORF15, while most missense mutations occur in a domain with homology to the protein RCC1, encoded by exons 1 10. Exon ORF15 is a hot spot for mutation, at least in the British population, in which it harbors 80% of the mutations found within a sample of 47 X-linked retinitis pigmentosa patients. Most RPGR mutations are unique to single families, which makes it difficult to demonstrate phenotype genotype correlations. Hum Mutat 19:486 500, 2002.

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“…In support of this view, a TBCC-related protein called retinitis pigmentosa 2 protein (RP2) localizes at the basal body of Trypanossoma brucei flagellum, where it was proposed to participate in a tubulin quality control mechanism prior to incorporation of tubulin heterodimers in the axoneme (108). In vertebrates, RP2 has been extensively studied due to its involvement in the X-linked condition retinitis pigmentosa, a pathology characterized by a progressive degeneration of photoreceptor cells (109,110). Similar to TBCC, RP2 also contains a TBCC and a CARP domain in its N-terminal region, suggesting a possible functional overlap between these two proteins.…”

Section: The Ciliary Roles Of Tubulin Folding Pathway Members and Relmentioning

confidence: 98%

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

Gonçalves¹,

Tavares²,

Carvalhal³

et al. 2010

BioMolecular Concepts

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Centrosomes and cilia are critical eukaryotic organelles which have been in the spotlight in recent years given their implication in a myriad of cellular and developmental processes. Despite their recognized importance and intense study, there are still many open questions about their biogenesis and function. In the present article, we review the existing data concerning members of the tubulin folding pathway and related proteins, which have been identified at centrosomes and cilia and were shown to have unexpected roles in these structures.

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Positional cloning of the gene for X-linked retinitis pigmentosa 2

Cited by 334 publications

References 33 publications

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

Mutations ofRPGR in X-linked retinitis pigmentosa (RP3)

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

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