Optogenetic tools for mammalian systems.

  • Lin J
  • Knutsen P
  • Muller A
 et al. 
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Channelrhodopsins (ChRs) are used to optogenetically depolarize neurons. We engineered a variant of ChR, denoted red-activatable ChR (ReaChR), that is optimally excited with orange to red light (λ ∼590-630 nm) and offers improved membrane trafficking, higher photocurrents and faster kinetics compared to existing red-shifted ChRs. Red light is less scattered by tissue and is absorbed less by blood than the blue to green wavelengths that are required by other ChR variants. We used ReaChR expressed in the vibrissa motor cortex to drive spiking and vibrissa motion in awake mice when excited with red light through intact skull. Precise vibrissa movements were evoked by expressing ReaChR in the facial motor nucleus in the brainstem and illumination with red light through the external auditory canal. Thus, ReaChR enables transcranial optical activation of neurons in deep brain structures without the need to surgically thin the skull, form a transcranial window or implant optical fibers.

Author-supplied keywords

  • Action Potentials
  • Action Potentials: physiology
  • Adaptor Proteins
  • Animals
  • Biosensing Techniques
  • Brain
  • Brain: physiology
  • Cell Membrane
  • Cell Membrane: metabolism
  • Cells
  • Cultured
  • Darkness
  • Eukaryotic Cells
  • Eukaryotic Cells: physiology
  • Female
  • Fluorescence
  • Genetic Variation
  • Genetic Variation: physiology
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Inbred C57BL
  • Inducible systems
  • Light
  • Luminescent Proteins
  • Luminescent Proteins: chemistry
  • Luminescent Proteins: genetics
  • Luminescent Proteins: metabolism
  • Male
  • Mice
  • Models
  • Molecular
  • Molecular Sequence Data
  • NIH 3T3 Cells
  • Native Polyacrylamide Gel Electrophoresis
  • Optical dimerisers
  • Optogenetics
  • Optogenetics: methods
  • Photic Stimulation
  • Photic Stimulation: methods
  • Photoreceptors
  • Protein Conformation
  • Protein Engineering
  • Protein Multimerization
  • Protein Structure
  • Pseudopodia
  • Pseudopodia: metabolism
  • Pseudopodia: ultrastructure
  • Rats
  • Recombinant Fusion Proteins
  • Recombinant Fusion Proteins: chemistry
  • Recombinant Fusion Proteins: genetics
  • Recombinant Fusion Proteins: metabolism
  • Rhodopsin
  • Rhodopsin: biosynthesis
  • Rhodopsin: genetics
  • Serine Endopeptidases
  • Serine Endopeptidases: chemistry
  • Serine Endopeptidases: genetics
  • Serine Endopeptidases: metabolism
  • Sprague-Dawley
  • Tertiary
  • Vesicular Transport
  • Vesicular Transport: chemistry
  • Vesicular Transport: genetics
  • Vesicular Transport: metabolism
  • Viral Nonstructural Proteins
  • Viral Nonstructural Proteins: chemistry
  • Viral Nonstructural Proteins: genetics
  • Viral Nonstructural Proteins: metabolism

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  • John Y Lin

  • Per Magne Knutsen

  • Arnaud Muller

  • David Kleinfeld

  • Roger Y Tsien

  • Joanna Mattis

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