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-Structure paper
タイトル | Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 45, Page eadd3677, Year 2022 |
掲載日 | 2022年11月11日 |
著者 | Dounia El Mazouni / Piet Gros / |
PubMed 要旨 | Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells ...Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells that enable vision. Here, we present single-particle cryo-electron microscopy structures of solubilized PRPH2-ROM1 heterodimers and higher-order oligomers. High-risk PRPH2 and ROM1 mutations causing blindness map to the protein-dimer interface. Cysteine bridges connect dimers forming positive-curved oligomers, whereas negative-curved oligomers were observed occasionally. Hexamers and octamers exhibit a secondary micelle that envelopes four carboxyl-terminal helices, supporting a potential role in membrane remodeling. Together, the data indicate multiple structures for PRPH2-ROM1 in creating and maintaining compartmentalization of photoreceptor cells. |
リンク | Sci Adv / PubMed:36351012 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 8.2 Å |
構造データ | EMDB-14991, PDB-7zw1: EMDB-15020: PRPH2-ROM1 octamer EMDB-15021: PRPH2-ROM1 tetramer EMDB-15023: PRPH2-ROM1 hexamer |
由来 |
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キーワード | MEMBRANE PROTEIN / PRPH2 / peripherin-2 / ROM1 / hetero-complex / tetraspanin |