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The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors.

Publication ,  Journal Article
Roepman, R; Bernoud-Hubac, N; Schick, DE; Maugeri, A; Berger, W; Ropers, HH; Cremers, FP; Ferreira, PA
Published in: Hum Mol Genet
September 1, 2000

Mutations in the retinitis pigmentosa GTPase regulator (RPGR) gene cause X-linked retinitis pigmentosa type 3 (RP3), a severe, progressive and degenerative retinal dystrophy eventually leading to complete blindness. RPGR is ubiquitously expressed, yet mutations in the RPGR gene lead to a retina-restricted phenotype. To date, all RP3 associated missense mutations that have been identified are located in the RCC1-homologous domain (RHD) of RPGR. To investigate the molecular pathogenesis of RP3, we screened retinal yeast two-hybrid libraries with the RHD of RPGR. We identified several alternatively spliced gene products, some with retina-restricted expression, that interact specifically with RPGR in vivo and in vitro. Thus, these proteins were named RPGR-interacting protein 1 (RPGRIP1) isoforms. They contain a C-terminal RPGR-interacting domain and stretches of variable coiled-coil domains homologous to proteins involved in vesicular trafficking. The interaction between RPGR and RPGRIP1 isoforms was impaired in vivo by RP3-associated mutations in RPGR. Moreover, RPGR and RPGRIP1 co-localize in the outer segment of rod photoreceptors, which is in full agreement with the retinitis pigmentosa phenotype observed in RP3 patients. The localization of RPGRIP1 at 14q11 makes it a strong candidate gene for RP16. These results provide a clue for the retina-specific pathogenesis in RP3, and hint towards the involvement of RPGR and RPGRIP1 in mediating vesicular transport-associated processes.

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Published In

Hum Mol Genet

DOI

ISSN

0964-6906

Publication Date

September 1, 2000

Volume

9

Issue

14

Start / End Page

2095 / 2105

Location

England

Related Subject Headings

  • Two-Hybrid System Techniques
  • Transcriptional Activation
  • Tissue Distribution
  • Temperature
  • Sequence Homology, Amino Acid
  • Reverse Transcriptase Polymerase Chain Reaction
  • Retinal Rod Photoreceptor Cells
  • Retina
  • Proteins
  • Protein Structure, Tertiary
 

Citation

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Roepman, R., Bernoud-Hubac, N., Schick, D. E., Maugeri, A., Berger, W., Ropers, H. H., … Ferreira, P. A. (2000). The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors. Hum Mol Genet, 9(14), 2095–2105. https://doi.org/10.1093/hmg/9.14.2095
Roepman, R., N. Bernoud-Hubac, D. E. Schick, A. Maugeri, W. Berger, H. H. Ropers, F. P. Cremers, and P. A. Ferreira. “The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors.Hum Mol Genet 9, no. 14 (September 1, 2000): 2095–2105. https://doi.org/10.1093/hmg/9.14.2095.
Roepman R, Bernoud-Hubac N, Schick DE, Maugeri A, Berger W, Ropers HH, et al. The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors. Hum Mol Genet. 2000 Sep 1;9(14):2095–105.
Roepman, R., et al. “The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors.Hum Mol Genet, vol. 9, no. 14, Sept. 2000, pp. 2095–105. Pubmed, doi:10.1093/hmg/9.14.2095.
Roepman R, Bernoud-Hubac N, Schick DE, Maugeri A, Berger W, Ropers HH, Cremers FP, Ferreira PA. The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel transport-like proteins in the outer segments of rod photoreceptors. Hum Mol Genet. 2000 Sep 1;9(14):2095–2105.
Journal cover image

Published In

Hum Mol Genet

DOI

ISSN

0964-6906

Publication Date

September 1, 2000

Volume

9

Issue

14

Start / End Page

2095 / 2105

Location

England

Related Subject Headings

  • Two-Hybrid System Techniques
  • Transcriptional Activation
  • Tissue Distribution
  • Temperature
  • Sequence Homology, Amino Acid
  • Reverse Transcriptase Polymerase Chain Reaction
  • Retinal Rod Photoreceptor Cells
  • Retina
  • Proteins
  • Protein Structure, Tertiary