+検索条件
-Structure paper
タイトル | Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina. |
---|---|
ジャーナル・号・ページ | J Cell Biol, Vol. 218, Issue 3, Page 1027-1038, Year 2019 |
掲載日 | 2019年3月4日 |
著者 | J Bernard Heymann / Camasamudram Vijayasarathy / Rick K Huang / Altaira D Dearborn / Paul A Sieving / Alasdair C Steven / |
PubMed 要旨 | Mutations in the retinal protein retinoschisin (RS1) cause progressive loss of vision in young males, a form of macular degeneration called X-linked retinoschisis (XLRS). We previously solved the ...Mutations in the retinal protein retinoschisin (RS1) cause progressive loss of vision in young males, a form of macular degeneration called X-linked retinoschisis (XLRS). We previously solved the structure of RS1, a 16-mer composed of paired back-to-back octameric rings. Here, we show by cryo-electron microscopy that RS1 16-mers can assemble into extensive branched networks. We classified the different configurations, finding four types of interaction between the RS1 molecules. The predominant configuration is a linear strand with a wavy appearance. Three less frequent types constitute the branch points of the network. In all cases, the "spikes" around the periphery of the double rings are involved in these interactions. In the linear strand, a loop (usually referred to as spike 1) occurs on both sides of the interface between neighboring molecules. Mutations in this loop suppress secretion, indicating the possibility of intracellular higher-order assembly. These observations suggest that branched networks of RS1 may play a stabilizing role in maintaining the integrity of the retina. |
リンク | J Cell Biol / PubMed:30630865 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 10.0 Å |
構造データ | EMDB-7907: |
由来 |
|