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TitleCryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis.
Journal, issue, pagesSci Adv, Vol. 8, Issue 45, Page eadd3677, Year 2022
Publish dateNov 11, 2022
AuthorsDounia El Mazouni / Piet Gros /
PubMed AbstractMammalian 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.
External linksSci Adv / PubMed:36351012 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 8.2 Å
Structure data

14991

7zw1

EMDB-14991, PDB-7zw1:
Human PRPH2-ROM1 hetero-dimer
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-15020: PRPH2-ROM1 octamer
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-15021: PRPH2-ROM1 tetramer
Method: EM (single particle) / Resolution: 8.2 Å

EMDB-15023: PRPH2-ROM1 hexamer
Method: EM (single particle) / Resolution: 7.6 Å

Source
  • homo sapiens (human)
  • lama (mammal)
KeywordsMEMBRANE PROTEIN / PRPH2 / peripherin-2 / ROM1 / hetero-complex / tetraspanin

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