期刊
HUMAN MOLECULAR GENETICS
卷 18, 期 5, 页码 797-808出版社
OXFORD UNIV PRESS
DOI: 10.1093/hmg/ddn406
关键词
-
资金
- National Institutes of Health [EY10609, EY018656, EY007361]
- Core Grant for Vision Research [EY12190]
- Foundation Fighting Blindness
- Knights Templar Eye Research Foundation
- NATIONAL EYE INSTITUTE [R01EY010609, P30EY012190, R55EY010609, R01EY018656, R01EY007361, R56EY010609] Funding Source: NIH RePORTER
It is commonly assumed that the ultrastructural organization of the rim region of outer segment (OS) discs in rods and lamellae in cones requires functional retinal degeneration slow/rod outer segment membrane protein 1 (Rds/Rom-1) complexes. Cysteine-150 (C150) in Rds has been implicated in intermolecular disulfide bonding essential for functional Rds complexes. Transgenic mice containing the Rds C150S mutation (C150S-Rds) failed to form higher-order Rds oligomers, although interactions between C150S-Rds and Rom-1 occurred in rods, but not in cones. C150S-Rds mice exhibited marked early-onset reductions in cone function and abnormal OS structure. In contrast, C150S-Rds expression in rods partly rescued the rds(+/-) phenotype. Although C150S-Rds was detected in the OSs in rods and cones, a substantial percentage of C150S-Rds and cone opsins were mislocalized to different cellular compartments in cones. The results of this study provide novel insights into the importance of C150 in Rds oligomerization and the differences in Rds requirements in rods versus cones. The apparent OS structural differences between rods and cones may cause cones to be more susceptible to the elimination of higher-order Rds/Rom-1 oligomers (e.g. as mediated by mutation of the Rds C150 residue).
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据