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Channelrhodopsins with distinct chromophores and binding patterns
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Journal Article
Channelrhodopsins with distinct chromophores and binding patterns
2024
Overview
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.
It is known that channelrhodopsins use all-trans retinal as chromophore for light activation. Here, the authors find that different channelrhodopsins utilize various forms of retinal in mammalian cells, which could inspire next-generation optogenetic tools.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 9/74
/ Binding
/ Channelrhodopsins - chemistry
/ Channelrhodopsins - genetics
/ Channelrhodopsins - metabolism
/ Chlamydomonas reinhardtii - genetics
/ Chlamydomonas reinhardtii - metabolism
/ Genetics
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Light
/ Mammals
/ Optics
/ Proteins
/ Retina
/ Science
