Human PRPH2-ROM1 hetero-dimer
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ABSTRACT:
SUBMITTER: Dounia El Mazouni
PROVIDER: EMPIAR-11482 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis.
El Mazouni Dounia D Gros Piet P
Science advances 20221109 45
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 o ...[more]
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