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Gene Review

RPGRIP1  -  retinitis pigmentosa GTPase regulator...

Homo sapiens

Synonyms: CORD13, LCA6, RGI1, RGRIP, RPGR-interacting protein 1, ...
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Disease relevance of RPGRIP1

  • Limited proteolysis differentially modulates the stability and subcellular localization of domains of RPGRIP1 that are distinctly affected by mutations in Leber's congenital amaurosis [1].
  • Younger patients with an AIPL1 or RPGRIP1 variation were found to have severely reduced vision [2].
  • RPGRIP is a strong candidate gene for causing human retinal degeneration [3].
  • The combined information from expression analysis and chromosomal localization allowed for the identification of potential candidate genes for retinal diseases (CORD8, CORD9) and syndromic blindness/deafness/renal defects [4].

High impact information on RPGRIP1

  • Most LCA-associated missense mutations in RPGRIP1 are located in a segment that encodes two C2 domains [5].
  • Previously published work showed that both proteins, RPGR and RPGRIP1, are present in the ciliary structure that connects the inner and outer segments of rod and cone photoreceptors [6].
  • Patients with RPGRIP1 mutations have a degeneration of both rod and cone photoreceptors, and, early in life, they experience a severe loss of central acuity, which leads to nystagmus [6].
  • RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin [7].
  • These results support distinct but complementary functions of RPGRIP1 isoforms in cytoskeletal-mediated processes in photoreceptors and amacrine neurons, and may explain the Leber phenotype linked to RPGRIP1 mutations in humans [8].

Biological context of RPGRIP1

  • This model revealed a potential Ca2+-binding site that was predicted to be disrupted by a missense mutation in RPGRIP1, which was previously identified in an LCA patient [5].
  • The human and bovine RPGRIP1 undergo alternative splicing [9].
  • RPGRIP1 encompasses 24 coding exons, nine of which are first described here with their corresponding exon-intron boundaries [10].
  • The tissue-specific expression of RPGRIP explains why mutations in the ubiquitously expressed RPGR confer a photoreceptor-specific phenotype [11].
  • Using the newly available canine genome sequence we sequenced RPGRIP1 in affected and carrier MLHDs and identified a 44-nucleotide insertion in exon 2 that alters the reading frame and introduces a premature stop codon [12].

Anatomical context of RPGRIP1

  • Moreover, recent reports are seemingly in disagreement on the localization of RPGR and RPGRIP in photoreceptors [13].
  • RPGRIP is also expressed in other neurons such as amacrine cells [13].
  • Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles [7].
  • RPGRIP is the only protein known to localize specifically in the photoreceptor connecting cilium [11].
  • When over-expressed in heterologous cell lines, RPGRIP appears in insoluble punctate and filamentous structures [11].

Associations of RPGRIP1 with chemical compounds

  • Based on the C2 domain of novel protein kinase C epsilon (PKC epsilon), we built a 3D-homology model for the C-terminal C2 domain of RPGRIP1 [5].

Physical interactions of RPGRIP1

  • The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood [7].

Other interactions of RPGRIP1


Analytical, diagnostic and therapeutic context of RPGRIP1

  • METHODS: Identification of alternative splice transcripts of murine and human RPGRIP1 was performed by reverse transcription-polymerase chain reaction (RT-PCR) [9].
  • The murine rpgrip1 isoforms were analyzed by immunoblot and immunocytochemistry analysis of murine retinas and transient transfected cultured cells [9].


  1. Limited proteolysis differentially modulates the stability and subcellular localization of domains of RPGRIP1 that are distinctly affected by mutations in Leber's congenital amaurosis. Lu, X., Guruju, M., Oswald, J., Ferreira, P.A. Hum. Mol. Genet. (2005) [Pubmed]
  2. Evaluation of genotype-phenotype associations in leber congenital amaurosis. Galvin, J.A., Fishman, G.A., Stone, E.M., Koenekoop, R.K. Retina (Philadelphia, Pa.) (2005) [Pubmed]
  3. Identification of a novel protein interacting with RPGR. Boylan, J.P., Wright, A.F. Hum. Mol. Genet. (2000) [Pubmed]
  4. Identification of preferentially expressed mRNAs in retina and cochlea. Maubaret, C., Delettre, C., Sola, S., Hamel, C.P. DNA Cell Biol. (2002) [Pubmed]
  5. Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations. Roepman, R., Letteboer, S.J., Arts, H.H., van Beersum, S.E., Lu, X., Krieger, E., Ferreira, P.A., Cremers, F.P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Null RPGRIP1 alleles in patients with Leber congenital amaurosis. Dryja, T.P., Adams, S.M., Grimsby, J.L., McGee, T.L., Hong, D.H., Li, T., Andréasson, S., Berson, E.L. Am. J. Hum. Genet. (2001) [Pubmed]
  7. RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin. Shu, X., Fry, A.M., Tulloch, B., Manson, F.D., Crabb, J.W., Khanna, H., Faragher, A.J., Lennon, A., He, S., Trojan, P., Giessl, A., Wolfrum, U., Vervoort, R., Swaroop, A., Wright, A.F. Hum. Mol. Genet. (2005) [Pubmed]
  8. RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons. Castagnet, P., Mavlyutov, T., Cai, Y., Zhong, F., Ferreira, P. Hum. Mol. Genet. (2003) [Pubmed]
  9. Identification of novel murine- and human-specific RPGRIP1 splice variants with distinct expression profiles and subcellular localization. Lu, X., Ferreira, P.A. Invest. Ophthalmol. Vis. Sci. (2005) [Pubmed]
  10. Complete exon-intron structure of the RPGR-interacting protein (RPGRIP1) gene allows the identification of mutations underlying Leber congenital amaurosis. Gerber, S., Perrault, I., Hanein, S., Barbet, F., Ducroq, D., Ghazi, I., Martin-Coignard, D., Leowski, C., Homfray, T., Dufier, J.L., Munnich, A., Kaplan, J., Rozet, J.M. Eur. J. Hum. Genet. (2001) [Pubmed]
  11. Retinitis pigmentosa GTPase regulator (RPGRr)-interacting protein is stably associated with the photoreceptor ciliary axoneme and anchors RPGR to the connecting cilium. Hong, D.H., Yue, G., Adamian, M., Li, T. J. Biol. Chem. (2001) [Pubmed]
  12. Canine RPGRIP1 mutation establishes cone-rod dystrophy in miniature longhaired dachshunds as a homologue of human Leber congenital amaurosis. Mellersh, C.S., Boursnell, M.E., Pettitt, L., Ryder, E.J., Holmes, N.G., Grafham, D., Forman, O.P., Sampson, J., Barnett, K.C., Blanton, S., Binns, M.M., Vaudin, M. Genomics (2006) [Pubmed]
  13. Species-specific subcellular localization of RPGR and RPGRIP isoforms: implications for the phenotypic variability of congenital retinopathies among species. Mavlyutov, T.A., Zhao, H., Ferreira, P.A. Hum. Mol. Genet. (2002) [Pubmed]
  14. The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors. Roepman, R., Bernoud-Hubac, N., Schick, D.E., Maugeri, A., Berger, W., Ropers, H.H., Cremers, F.P., Ferreira, P.A. Hum. Mol. Genet. (2000) [Pubmed]
  15. Clinical phenotypes in carriers of Leber congenital amaurosis mutations. Galvin, J.A., Fishman, G.A., Stone, E.M., Koenekoop, R.K. Ophthalmology (2005) [Pubmed]
  16. Identification of mutations in the AIPL1, CRB1, GUCY2D, RPE65, and RPGRIP1 genes in patients with juvenile retinitis pigmentosa. Booij, J.C., Florijn, R.J., ten Brink, J.B., Loves, W., Meire, F., van Schooneveld, M.J., de Jong, P.T., Bergen, A.A. J. Med. Genet. (2005) [Pubmed]
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