Channelrhodopsins with distinct chromophores and binding patterns.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
24 Aug 2024
24 Aug 2024
Historique:
received:
03
10
2023
accepted:
16
08
2024
medline:
26
8
2024
pubmed:
26
8
2024
entrez:
24
8
2024
Statut:
epublish
Résumé
Channelrhodopsins are popular optogenetic tools in neuroscience, but remain poorly understood mechanistically. Here we report the cryo-EM structures of channelrhodopsin-2 (ChR2) from Chlamydomonas reinhardtii and H. catenoides kalium channelrhodopsin (KCR1). We show that ChR2 recruits an endogenous N-retinylidene-PE-like molecule to a previously unidentified lateral retinal binding pocket, exhibiting a reduced light response in HEK293 cells. In contrast, H. catenoides kalium channelrhodopsin (KCR1) binds an endogenous retinal in its canonical retinal binding pocket under identical condition. However, exogenous ATR reduces the photocurrent magnitude of wild type KCR1 and also inhibits its leaky mutant C110T. Our results uncover diverse retinal chromophores with distinct binding patterns for channelrhodopsins in mammalian cells, which may further inspire next generation optogenetics for complex tasks such as cell fate control.
Identifiants
pubmed: 39181878
doi: 10.1038/s41467-024-51811-x
pii: 10.1038/s41467-024-51811-x
doi:
Substances chimiques
Channelrhodopsins
0
Retinaldehyde
RR725D715M
Rhodopsin
9009-81-8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7292Informations de copyright
© 2024. The Author(s).
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