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  NYX (Nyctalopin on chromosome X), the gene mutated in congenital stationary night blindness, encodes a cell surface protein

Zeitz, C., Scherthan, H., Freier, S., Feil, S., Suckow, V., Schweiger, S., et al. (2003). NYX (Nyctalopin on chromosome X), the gene mutated in congenital stationary night blindness, encodes a cell surface protein. Investigative Ophthalmology & Visual Science, 44(10), 4184-4191. doi:10.1167/iovs.03-0251.

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Genre: Journal Article
Alternative Title : Invest. Ophthalmol. Vis. Sci.

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 Creators:
Zeitz, Christina1, Author
Scherthan, Harry2, Author           
Freier, Susanne2, Author           
Feil, Silke1, Author
Suckow, Vanessa3, Author           
Schweiger, Susann2, Author           
Berger, Wolfgang2, Author           
Affiliations:
1Max Planck Society, ou_persistent13              
2Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433549              
3Signal Transduction in Mental Retardation and Pain (Tim Hucho), Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479646              

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 Abstract: PURPOSE. The complete type of X-linked congenital stationary night blindness (CSNB1) in human and mouse is caused by mutations in the NYX gene. The human NYX protein has been predicted to contain an N-terminal endoplasmic reticulum (ER) signaling sequence and a C-terminal glycosylphosphatidylinositol (GPI) anchor. In the current study, these computer predictions were verified experimentally by expression of domain-specific cDNA constructs in COS-7 and HeLa cells. Moreover, computer-based analysis of the orthologue mouse amino acid sequence did not reveal a GPI anchor, which may result in a different protein localization compared with human NYX. Therefore, the cellular localization for the mouse Nyx protein was also examined. METHODS. A new method was established that differentially visualizes both the protein at the surface of the living cell and subsequently in intracellular compartments. The localization of the human and mouse V5-tagged wild-type and mutant NYX protein were studied. RESULTS. Human and mouse V5-NYX proteins were dispersed in the form of speckles over the entire cell surface. Subsequent staining of the same cells after detergent extraction revealed that V5-NYX located to the ER and Golgi apparatus. Deletion of the GPI anchor domain of NYX resulted in a time-dependent loss of V5-NYX from the surface of living cells and accumulation of this truncated protein in the ER and Golgi apparatus. Deletion of the ER signal sequence in Nyx delocalized the intracellular V5-Nyx protein and caused its dispersion in the cytosol. Furthermore, mutations introduced in the leucine-rich repeat (LRR)-region, which has been described as a pathogenic variant of NYX, had no effect on subcellular localization of the protein. CONCLUSIONS. These data provide evidence that human and mouse nyctalopin are membrane-bound extracellular proteins and are functionally conserved.

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Language(s): eng - English
 Dates: 2003-10
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: eDoc: 173655
ISI: 000185636700004
DOI: 10.1167/iovs.03-0251
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Title: Investigative Ophthalmology & Visual Science
  Alternative Title : Invest. Ophthalmol. Vis. Sci.
Source Genre: Journal
 Creator(s):
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Pages: - Volume / Issue: 44 (10) Sequence Number: - Start / End Page: 4184 - 4191 Identifier: ISSN: 0146-0404