Dynamics of the Rhomboid-like Protein RHBDD2 Expression in Mouse Retina and Involvement of Its Human Ortholog in Retinitis Pigmentosa
| Autor: | Donald A. Fox, Rıza Köksal Özgül, Emmanuel Mendoza, J. E. Johnson, Clyde K. Yamashita, Novruz B. Ahmedli, Collins C. Njoku, Akash Naidu, Alejandra Young, Yekaterina E. Gribanova, Debora B. Farber |
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| Rok vydání: | 2013 |
| Předmět: |
Opsin
Amino Acid Motifs Molecular Sequence Data Glycine Golgi Apparatus Biology Biochemistry Regulated Intramembrane Proteolysis Retina Mice symbols.namesake Pregnancy Endopeptidases Retinitis pigmentosa medicine Animals Humans Amino Acid Sequence Golgi localization Molecular Biology In Situ Hybridization Opsins Sequence Homology Amino Acid Rhomboid Cell Membrane Homozygote Gene Expression Regulation Developmental Membrane Proteins Cell Biology Golgi apparatus medicine.disease Immunohistochemistry Molecular biology Neoplasm Proteins Mice Inbred C57BL Transmembrane domain HEK293 Cells Gene Expression Regulation Membrane protein Mutation Mutagenesis Site-Directed Retinal Cone Photoreceptor Cells symbols Pregnancy Animal Female sense organs Retinitis Pigmentosa |
| Zdroj: | Journal of Biological Chemistry. 288:9742-9754 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m112.419960 |
| Popis: | The novel rhomboid-like protein RHBDD2 is distantly related to rhomboid proteins, a group of highly specialized membrane-bound proteases that catalyze regulated intramembrane proteolysis. In retina, RHBDD2 is expressed from embryonic stages to adulthood, and its levels show age-dependent changes. RHBDD2 is distinctly abundant in the perinuclear region of cells, and it localizes to their Golgi. A glycine zipper motif present in one of the transmembrane domains of RHBDD2 is important for its packing into the Golgi membranes. Its deletion causes dislodgment of RHBDD2 from the Golgi. A specific antibody against RHBDD2 recognizes two forms of the protein, one with low (39 kDa; RHBDD2(L)) and the other with high (117 kDa; RHBDD2H) molecular masses in mouse retinal extracts. RHBDD2(L) seems to be ubiquitously expressed in all retinal cells. In contrast, RHBDD2H seems to be present only in the outer segments of cone photoreceptors and may correspond to a homotrimer of RHBDD2(L). This protein consistently co-localizes with S- and M-types of cone opsins. We identified a homozygous mutation in the human RHBDD2 gene, R85H, that co-segregates with disease in affected members of a family with autosomal recessive retinitis pigmentosa. Our findings suggest that the RHBDD2 protein plays important roles in the development and normal function of the retina. |
| Databáze: | OpenAIRE |
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