Channelrhodopsins

From OpenOptogenetics.org

Jump to: navigation, search

Fig. 1. From [1].
Fig. 2. Channelrhodopsin-2 is activated by photoisomerization of all-trans retinal to 13-cis retinal at wavelengths of 470 nm. After photoisomerization, the covalently bound retinal spontaneously relaxes to all-trans in the dark, providing closure of the ion channel and regeneration of the chromophore. From [1].

Channelrhodopsins (ChRs) are directly light-gated ion channels originating from microalgae of the genus Chlamydomonas. They are larger than any other rhodopsin with a 7 transmembrane (7TM) region and a long C-terminal extension (Fig. 1). In algae they function as visual proteins directing the alga towards or away from a light source and to find light conditions that are optimal for photosynthetic growth. The 7TM region shows some homology to other microbial (procaryotic) rhodopsins functioning as light-driven pumps (bacteriorhodopsin, archeorhodopsin and halorhodopsin) or sensors. The 7TM part of ChR is sufficient for the channel function and is used for all optogenetic applications. The vitamin A derivative retinal is linked to a lysine residue of the proteins (Retinal Schiff Base, RSB) constituting the light absorbing chromophore. Retinal is available in sufficient amounts in nearly all neuronal cells of mammals. Light absorption causes retinal isomerization around the 13-bond. This isomerization triggers subsequent conformational changes of the protein and gating of the channel. Thermal relaxation of the proteins closes the channel and the protein converts under reisomerization of the retinal back to the dark state. ChR2 from Chlamydomonas reinhardtii has been established as the ChR prototype for optogenetic application since it is more than 10 times better expressed in most host cells than the earlier found ChR1.

Engineering of the ChRs or the generation of hybrids allows to modify spectral and kinetic properties of ChRs but also to improve expression and membrane targeting in host cells. Owing to the fact that the retinal-binding pocket is conserved in all microbial rhodopsins, the first amino acids to be modified were the ones located in close contact with the retinal. Replacement of the active site residue E123 by Thr and Ala (ChETA variants) caused faster channel closing, eliminated the voltage sensitivity of the temporal kinetics, and induced a 20 nm bathochromic shift [2]. In contrast, substitution of C128 by Ser, or of D156 by Ala or combination of both lead to an extreme extension of the open state lifetime with τoff values up to 30 minutes and allowed on/off switching with dual wavelength light protocols [3, 4, 5]. Mutation of E90, E123, L132, or H134 does not change photocycle kinetics but alters ion selectivity in favor of H+, Na+ or Ca2+, or reduces inactivation after light step-up or multiple light flashes, respectively ([6] and Kleinlogel 2011). A helix swapping approach combining structural elements from ChR1 and ChR2 led to improved ChRs with larger currents, absorption maxima around 500 nm and reduced inactivation [7].

Links

Reviews

Naturally occurring channelrhodopsins

Phylogenetic tree of the 7TM domains of the so far known channelrhodopsins constructed by the neighbor-joining method. From [8].
Genus Species Channelrhodospin Accession # Refs
Clamydomonas reinhardtii ChR1
ChR2
augustae CaChR1 [8]
yellowstonensis CyChR1 [8]
raudensis CraChR2 [8]
Volvox carteri VChR1
VChR2
Mesostigma viride MChR1 [9]
Haematococcus pluvialis HpChR1
Dunaliella salina DChR1 [10]
Pleodorina starrii PsChR1 [10]
Pleodorina starrii PsChR2 [10]
Pyramimonas gelidicola PgChR1 [10]

Mutagenesis

Evaluation of different ChR2 variants for use in pyramidal neurons. Photocurrent amplitude and channel speed, defined as 1/(flash to peak + τoff) determine the performance in neurons. The ideal ChR should gate large currents with rapid kinetics (green shaded corner). From [11]
Three-dimensional computer model of ChR2. Mutations of the amino acid residues shown in stick representation are known to substantially influence absorption, conductance (without selectivity change), kinetics and ion selectivity, as indicated for each residue. The retinal moiety is shown in yellow, residues conserved in all four known channelrhodopsins are colored blue, and residues that differ in various channelrhodopsins are colored gray. Oxygen, nitrogen and sulfur atoms are colored red, blue and dark yellow, respectively. Graphics are based on the coordinates of H. salinarum bacteriorhodopsin [12] and were drawn with Pymol (Schrödinger). From Hegemann and Möglich, 2011.

Rationale

The work on Channelrhodospin variants aims at tweaking 3 major properties:

  • Increasing the peak and steady-state photocurrents by increasing light sensitivity and/or unitary conductances.
  • Speeding up or slowing down the duration of the photocycle.
  • Shifting the peak sensitivity toward longer wavelengths (red).

Key positions

Channelrhodopsin variants have been engineered from a small number of original proteins isolated from the unicellular green algae Chlamydomonas reinhardtii (ChR1 and ChR2) and Volvox carteri (VChR1 and VChR2). These variants have been obtained through mutagenesis and chimerization. A few key positions in ChR2 have been identified so far:

  • position 123. Mutations at this position ("ChETA" mutations, e.g. E123T and E123A) significantly accelerate the open state decay (i.e. faster deactivation kinetics) but reduce photocurrent amplitudes compared to wild-type ChR2.
  • position 128. Mutation at this position (e.g. C128T, C128S, C128A) can extend the open state life time, up to seconds or even minutes. C128 mutants are often called SFOs (step-function opsins).
  • position 134. The H134R mutation generates larger photocurrents than wild-type ChR2, but slows down channel kinetics.
  • position 159. The T159C mutant displays increased photocurrents (slightly higher than the H134R mutation).

Available variants

Color code:

  • = variant excited by blue/green light.
  • = red-shifted variant (yellow/red light).
  • = ChETA mutants (fast deactivation kinetics).
  • = slow cycling ChR a.k.a step function opsin (SFO): mutants converting a brief pulse of light into a stable step in membrane potential.
  • Χ = chimera (hybrids).


Acronym & name Description Accession # Refs
ChR1 (Channelrhodopsin-1) ChR1 is a directly light-gated ion channel of the green alga Chlamydomonas reinhardtii (http://www.chlamy.org/). In most Chlamydomonas strains ChR1 is the dominant ChR. ChR1 is highly selective for protons but under physiological pH with low proton abundance it also conducts cations like Na+, K+, and Ca++. The preference for H+ over Na+ is about 10E6 fold. It shows a strong pH dependence of the absorption spectrum. [13]
ChR2 (Channelrhodopsin-2) ChR2 is the second light-gated ion channel of Chlamydomonas reinhardtii. The cation selectivity is two fold high compared to ChR1 but the expression in most host cells is > 10 times better than ChR1. Thus ChR2 has been established as the paradigm in Optogenetics. [14]
VChR1 (Volvox-Channelrhodopsin-1) VChR1 is the main ChR of the colonial alga Volvox carteri. Expression in neurons is roughly 3 times lowers than that of ChR2 but still allowed action potential firing with 589 nm light. Expression too low in other neuronal cells. pH-dependence of the absorption. Zhang et al. 2008, [15]
VChR1(C123S) (VChR1-SFOs) Slow cycling ChR a.k.a Step Function Opsin (SFO) VChR1 with 32 seconds open state life time.
VChR1(C123S/D151A) (VChR1-SFOs) Slow cycling ChR a.k.a Step Function Opsin (SFO) VChR1 with 5 min open state life time.
MChR1 (Channelrhodopsin from Mesostigma viride) [9]
VChR2 (Volvox-Channelrhodopsin-2) VChR2 is the second ChR of the colonial alga Volvox carteri. Expression in neurons is lowers than that of ChR2. Expression too low in other neuronal cells. Low pH-dependence of the absorption. [15]
ChD
ChR2(H134R) Channelrhodopsin-2 mutant H134R ChR2(H134R) shows a 2 fold extended open state life time; 2 fold higher Na+-selectivity. 2 fold lower degree of inactivation. Good expression in neurons. [16]
ChEF (Channelrhodopsin-1/2 hybrid) Hybrid of ChR1 and ChR2, C1C2-2,5

weak inactivation, large currents in oocytes and HEK-cells; tends to aggregate in neurons, extended open state life time

[16]
Χ ChIEF (Channelrhodopsin-1/2 hybrid) Hybrid of ChR1 and ChR2, C1C2-2,5 with additional L170I mutation (ChR1 numbering) or at L131I (ChR2-numbering)

weak inactivation, large currents in oocytes and HEK-cells; sometimes tends to aggregate in neurons, almost wild type like open state life time

[16]
ChR2(L132C) (CatCh) (Calcium translocating channelrhodopsin) The L132C mutation (located in the third transmembrane domain) yielded the following changes compared with the wild type ChR2 (measured in cultured hippocampal neurons unless mentioned): 3.5-fold increased current amplitudes, 10-fold increased light sensitivity, 1.6-fold increased PCa/PNa relative permeability (HEK293 cells). Kleinlogel et al. 2011
ChR2(T159C) (TC) (Channelrhodopsin-2 mutant T159C) [11]
Χ ChRWR Channelrhodopsin-wide receiver) ChRWR is sensitive to wavelengths of 480–540 nm, has large effective conductance when expressed in HEK293 cells, and its photocurrent desensitization was almost negligible. Its ON and OFF kinetics are the same as those of ChR2. [7]
Χ ChRFR Channelrhodopsin-fast receiver) ChRFR has fast ON and OFF kinetics and is also characterized by small desensitization and large effective conductance. [7]
Χ ChRGR (Channelrhodopsin-green receiver) ChRGR was obtained by replacing one subdomain of the 6th transmembrane helix of ChR1 (residues 297-345) by its counterpart from ChR2 (residues 258-315). ChRGR displays a greater conductance and less desensitization than ChR1, rapid ON and OFF kinetics and larger photocurrents than VChR1 @ 520 nm. The absorption maximum is near 505 nm. pH sensitivity of the absorption has not been described in detail.
Χ C1V1 C1V1 was obtained by fusing the N-terminal sequence of the ChR1 coding sequence with the C-terminal sequence of VChR1. C1V1 displays maximum absorption at 540 nm and apparent off-kinetic of 130 ms. [5]
Χ C1V1(E162T) Shows a maximum absorption at 530 nm and a hypsochromic shoulder making the absorption spectra unusually broad.

Off-kinetics is half of C1V1 (60 ms)

[5]
Χ C1V1(E122T) High-efficient in neurons. Red-shifted compared to C1V1 to 550 nm. Has moderated off-kinetic with 130 ms. [5]
Χ C1V1(S220G) Maximum absorption at 526 nm with a narrow actions spectra and a moderate off-kinetics off 122 ms. [17]
Χ C1V1(E122T/E162T) High-efficient in neurons. Maximum absorption at 530 with a narrow actions spectra. Off-kinetics is 35 ms. [5]
Χ C1V1-triple (E122T/V196I/G197A) Red-shifted absorption at 544 nm with a realtively fast off-kinetic at 41 ms. Varied expression in different organism. [17]
ChR2(E123T) (ChETA) Channelrhodopsin-2 mutant E123T ChR2 with mutated Retinal Schiff Base counter ion, more than 2 fold accelerated open state decay ( 5 ms) and voltage independent kinetics. Ideal for fast neuronal action potential firing, especially in interneurons. The absorption maximum is shifted to 495 nm. [18]
ChR2(E123A) (ChETA-b) Channelrhodopsin-2 mutant E123A ChR2 with mutated Retinal Schiff Base counter ion, more than 2 fold accelerated open state decay ( 4 ms) and voltage independent kinetics. Ideal for fast neuronal action potential firing, especially in interneurons. Expression is better than E123T in some cell types but may be lower in others. Spectral Maximum near 485 nm. Described in Guanaydin2010 Suppl. [18]
ChR2(E123T/T159C) (ET/TC) Channelrhodopsin-2 double mutant E123T and T159C ET/TC mutants display both enhanced photocurrents and faster kinetics, with the highest speed/photocurrent combination achieved so far. They enable reliable and sustained optical stimulation of hippocampal pyramidal neurons up to 60 Hz. [11]
ChR2(L132C/T159C) (LC/TC) Channelrhodopsin-2 double mutant L132C and T159C This variants combines good expression of T159C with small inactivation and higher calcium permeability of L132C. Photocurrent amplitudes are 3nA in Hek cells making LC/TC the best expressing ChR so far. Off-kinetic is 109 ms and maximal absorption is 460 nm. [17]
ChR2(C128T) Channelrhodopsin-2 mutant C128T Slow cycling ChR a.k.a Step Function Opsin (SFO) with 2 seconds open state life time. Strong expression in hippocampal neurons and Pichia pastoris. Inactivates at strong light due to reaction into a deprotonated species. D128 is part of the DC gate. [3][19]
ChR2(C128A) Channelrhodopsin-2 mutant C128A Slow cycling ChR a.k.a Step Function Opsin (SFO) with 42 seconds open state life time, weak expression in hippocampal neurons and Pichia pastoris. [3][19]
ChR2(C128S) Channelrhodopsin-2 mutant C128S Slow cycling ChR a.k.a Step Function Opsin (SFO) with 1.7 min open state life time, moderate expression in hippocampal neurons and Pichia pastoris. Inactivates at strong light due to reaction into a deprotonated species. [3][19]
ChR2(D156A) Channelrhodopsin-2 mutant D156A Slow cycling ChR a.k.a Step Function Opsin (SFO) with 6.9 min open state life time. D156 is part of the DC gate. [20]
ChR2(C128S/D156A) Channelrhodopsin-2 mutant C128S/D156A Stabilized Step Function Opsin (SSFO) with 29 min open state life time. D156 is part of the DC gate. [20]
ChRs with specific intracellular localization
ChR2-MBD Fusion between ChR2 and the Myosin Va–binding domain of Melanophilin. Localized to the somatodendritic tree. [21]
ChR2-EYFP-ETQV Fusion between ChR2 and the PDZ-domain binding sequence ETQV, a motif involved in NMDA receptor clustering at postsynaptic sites. Preferential localization to post-synaptic densities. [22]
ChR2-YFP-Na(v)II-III Fusion between Channelrhodopsin-2 and the the ankyrinG-binding loop of voltage-gated sodium channels (Na(v)II-III). Localized to the initial segment. [23, 24]
Opsin fusions
ChR2-EYFP-βbR Fusion between Channelrhodopsin-2 and bacteriorhodopsin. JN836740 Kleinlogel et al, 2011
ChR2-EYFP-βNphR Fusion between Channelrhodopsin-2 and halorhodopsin. JN836741 Kleinlogel et al, 2011
hChR2(H134R)-mKate-h(β-bR) Fusion between Channelrhodopsin-2(H134R) and bacteriorhodopsin. JN836742 Kleinlogel et al, 2011
hChR2(D156A)-mKate-h(β-bR) Fusion between Channelrhodopsin-2(D156A) and bacteriorhodopsin. JN836744 Kleinlogel et al, 2011
hVChR1-mKate-β-hChR2 Fusion between humanized VChR1 and humanized ChR2. JN836745 Kleinlogel et al, 2011
hVChR1-mKate-β-hChR2(L132C) Fusion between humanized VChR1 and humanized ChR2(L132C). JN836746 Kleinlogel et al, 2011
ChR2-EYFP-β-Arch Fusion between ChR2 and archaerhodopsin-3. JN836747 Kleinlogel et al, 2011

Properties of available variants

Kinetic and spectral attributes of channelrhodopsin variants, light-driven pumps (see Light-driven pumps) and and opto-XRs (see Opto-XRs). From [25]

The values in the table below were compiled from [26], [27] and [25]. Color code:

  • = variant excited by blue/green light.
  • = red-shifted variant (yellow/red light).
  • = ChETA mutants (fast deactivation kinetics).
  • = step-function opsin (bistable modulation).


Acronym λ max** (nm) Desensitization*** (1 - Is-s/Ipeak) Sensitivity (EC50) (mW/mm2) τon (opening rate, in ms) τoff (closing rate) Estimated unitary g (fS) Refs
peak steady-state peak steady-state
ChR1 [14]
ChR2 470 450 0.88 @ 470 nm (pHo=7.5, -100 mV) 1.10 1.05 1.21 @ 20 mW/mm2 ~10 ms [28, 29, 30, 31]
VChR2 470 470 0.70 @ 470 nm
ChD 450 450 0.69 @ 470 nm 3.23 1.02 1.49 @ 20 mW/mm2 7.82 ms
ChR2(H134R) 450 450 0.61 @ 470 nm 1.07 0.98 1.92 @ 20 mW/mm2 18 ms [16]
ChEF 470 490 0.30 @ 470 nm 0.72 0.46 1.56 @ 20 mW/mm2 24.9 ms
ChIEF 450 450 0.20 @ 470 nm 1.65 1.38 1.62 @ 20 mW/mm2 ~10 ms
ChR2(L132C) (CatCh) 16 ms Kleinlogel et al., 2011
ChR2(T159C) (TC) 26 ms [11]
ChRGR 4-5 ms [32]
ChR2(E123T) (ChETA) 490 nm 0.76 @ 470 nm 5.02 0.62 0.86 @ 20 mW/mm2 4.4 ms [2]
ChR2(E123A) (ChETA-b) 4 ms
ChR2(E123T/T159C) (ET/TC) 8 ms
ChR2(C128T) 2 s [3]
VChR1(C123S) 32 s
ChR2(C128A) 42 s [3]
ChR2(C128S) 1.7 min [3]
VChR1(C123S/D151A) 5 min
ChR2(D156A) 6.9 min
ChR2(C128S/D156A) 29 min
VChR1 535-545 535-545 0.52 @ 535 nm Not tested Not tested 2.8 @ 15 mW/mm2 133 ms [33]
MChR1
C1V1 156 ms
C1V1(E162T) 58 ms
C1V1(E122T/E162T) 34 ms

List of Available Constructs

pcDNAs

Name Description Map Lab Addgene
p-hChR2-mCherry humanized ChR2 (1 -308aa) Map (everyvector) Hegemann Lab
p-hChR2-mCherry (H134R) humanized ChR2 (1 -308aa) Map (everyvector) Hegemann Lab
p-hChR2-mCherry (C128T) humanized ChR2 (1 -308aa) Map (everyvector) Hegemann Lab
p-hChR1-eCFP humanized VChR1 (1 - 356aa) Map (everyvector) Hegemann Lab
p-hVChR1-eCFP humanized VChR1 (1 - 316aa) Map (everyvector) Hegemann Lab
p-hVChR2-eGFP humanized VChR2 (1 - 308aa) Map (everyvector) Hegemann Lab
p-C1V1-eCFP (B Variante/Neuronen) humanized C1V1 2L5 (1 - 360aa) Map (everyvector) Hegemann Lab
p-C1V1-ETET-eCFP (B Variante/Neuronen) humanized C1V1 2L5 E122T E162T (1 - 360aa) Map (everyvector) Hegemann Lab
p-C1V1-S220G-eCFP (A Variante/Neuronen) humanized C1V1 25 S220G (1 - 360aa) Map (everyvector) Hegemann Lab
p-C1V1-triple-eCFP (A Variante/Neuronen) humanized C1V1 25 E122T V196I G197A (1 - 360aa) Map (everyvector) Hegemann Lab
p-hChR2-L132C-T159C-mCherry (C128T) humanized ChR2 L132C T159C (1 -308aa) Map (everyvector) Hegemann Lab
pcDNA3.1/hChR2(H134R)-EYFP Deisseroth lab Plasmid 20940
pcDNA3.1/hChR2(H134R)-mCherry Deisseroth lab Plasmid 20938
pcDNA3.1/hChR2-EYFP Deisseroth lab Plasmid 20939
pcDNA3.1/VChR1-EYFP Deisseroth lab Plasmid 20955

AAV Plasmids

DiO plasmids

The DiO (Double-floxed Inverted ORF) strategy is also known as the flip-excision (FLEX) switch and was first described in [34].

Name Description Map Lab Addgene
pAAV-Ef1a-DIO-ChETA-EYFP humanized ChR2 with H134R mutation to achieve higher currents and E123T (ChETA) mutation to accelerate open state decay. everyvector.com Deisseroth lab Plasmid 26968
pAAV-EF1a-double floxed-hChR2(H134R)-EYFP-WPRE-HGHpA humanized ChR2 with H134R mutation to achieve higher currents. Deisseroth lab Plasmid 20298
pAAV-EF1a-double floxed-hChR2(H134R)-mCherry-WPRE-HGHpA humanized ChR2 with H134R mutation to achieve higher currents. Deisseroth lab Plasmid 20297
pAAVs with YFP only (for control experiments)
pAAV-Ef1a-DIO EYFP Deisseroth lab Plasmid 27056
pAAV-EF1a-double floxed-EYFP-WPRE-HGHpA Deisseroth lab Plasmid 20296
pAAV-EF1a-double floxed-mCherry-WPRE-HGHpA Deisseroth lab Plasmid 20299

Plasmids with specific promoters

Name Description Map Lab Addgene
pAAV-CaMKIIa-hChR2(H134R)-EYFP hChR2 (humanized ChR2) H134R mutant. Deisseroth lab Plasmid 26969
pAAV-CaMKIIa-hChR2(H134R)-mCherry hChR2 (humanized ChR2) H134R mutant. Deisseroth lab Plasmid 26975
pAAV-GFAP-hChR2(H134R)-EYFP hChR2 (humanized ChR2) H134R mutant. Deisseroth lab Plasmid 27054
pAAV-GFAP-hChR2(H134R)-mCherry hChR2 (humanized ChR2) H134R mutant. Deisseroth lab Plasmid 27055
pAAV-hSyn-hChR2(H134R)-EYFP hChR2 (humanized ChR2) H134R mutant. Deisseroth lab Plasmid 26973
pAAV-hSyn-hChR2(H134R)-mCherry hChR2 (humanized ChR2) H134R mutant. Deisseroth lab Plasmid 26976

Lentivirus Plasmids

Plasmids with specific promoters

Name Description Map Lab Addgene
ChETA mutants (fast deactivation kinetics)
pLenti-CaMKIIa-ChETA-EYFP Deisseroth lab Plasmid 26967
SFOs (Step Function Opsins)
Mutants converting a brief pulse of light into a stable step in membrane potential
pLenti-CaMKIIa-hChR2(C128A)-EYFP-WPRE Deisseroth lab Plasmid 20293
pLenti-CaMKIIa-hChR2(C128S)-EYFP-WPRE Deisseroth lab Plasmid 20294
pLenti-CaMKIIa-hChR2(C128T)-EYFP-WPRE Deisseroth lab Plasmid 20295
humanized ChR2 with H134R mutation to achieve higher currents
pLenti-CaMKIIa-hChR2(H134R)-EYFP-WPRE Deisseroth lab Plasmid 20944
pLenti-CaMKIIa-hChR2(H134R)-mCherry-WPRE Deisseroth lab Plasmid 20943
pLenti-Synapsin-hChR2(H134R)-EYFP-WPRE Deisseroth lab Plasmid 20945
Volvox-Channelrhodopsin-1
pLenti-CaMKIIa-VChR1-EYFP-WPRE Deisseroth lab Plasmid 20954

List of available transgenic lines

Strain Name Type Description Lab Jackson Labs stock # Ref
ChR2
B6.Cg-Tg(Thy1-COP4/EYFP)18Gfng/J This line (founder line 18) has the expression of ChR2::YFP directed to neural cells by the the murine thymus cell antigen 1 (Thy1) promoter region. Expression is observed throughout the brain, including the cortex, hippocampus, thalamus, midbrain, brainstem, cerebellar mossy fibers, and retinal ganglion cells. Guoping Feng 007612
B6.Cg-Tg(Thy1-COP4/EYFP)9Gfng/J This line (founder line 9) has the expression of ChR2::YFP directed to neural cells by the the murine thymus cell antigen 1 (Thy1) promoter region. Expression is observed in layer 5 cortical neurons, CA1 and CA3 pyramidal neurons of the hippocampus, cerebellar mossy fibers, neurons in the thalamus, midbrain and brainstem, and the olfactory bulb mitral cells. Guoping Feng 007615
B6;SJL-Tg(Thy1-COP4*H134R/EYFP)20Gfng/J This line (founder line 20) has the expression of hChR2(H134R)::YFP directed to neural cells by the murine thymus cell antigen 1 (Thy1) promoter region. Guoping Feng 012350
Vglut2-ChR2-YFP BAC This line has the expression of ChR2::YFP directed to a subset of glutamatergic neurons by the vesicular glutamate transporter 2 (Vglut2) promoter. Ole Kiehn Hägglund et al., 2010.
ChAT-ChR2-EYFP BAC This line has the expression of ChR2::YFP directed to cholinergic neurons by the choline acetyltransferase (ChAT) promoter. Guoping Feng 014545 and 014546 [35]
VGAT-ChR2-EYFP BAC This line has the expression of ChR2::YFP directed to GABAergic neurons by the vesicular GABA transported (VGAT) promoter. Guoping Feng 014548
TPH2-ChR2-EYFP BAC This line has the expression of ChR2::YFP directed to serotonergic neurons by thetryptophan hydroxylase 2 (TPH2) promoter. Guoping Feng 014555
B6;SJL-Tg(Pvalb-COP4*H134R/EYFP)15Gfng/J BAC This line has the expression of hChR2(H134R)::YFP directed to parvalbumin-positive neurons by the parvalbumin (PV) promoter/enhancer. Guoping Feng 012355
ChR2 "reporter" strains
B6.Cg-Gt(ROSA)26Sor<tm27.1(CAG-COP4*H134R/tdTomato)Hze>/J These Ai27D (or Ai27ΔNeo) mice conditionally express an improved channelrhodopsin-2/tdTomato fusion protein (hChR2(H134R)-tdTomato) from the endogenous Gt(ROSA)26Sor locus. Expression is enhanced by the presence of a CAG promoter. Following Cre-mediated removal of the floxed STOP cassette, these mice can be used in optogenetic studies for rapid in vivo activation of excitable cells by illumination with blue light (450-490 nm). Allen Institute 012567
B6;129S-Gt(ROSA)26Sor<tm32.1(CAG-COP4*H134R/EYFP)Hze>/J These Ai32 mice conditionally express an improved channelrhodopsin-2/EYFP fusion protein (ChR2(H134R)-EYFP) from the endogenous Gt(ROSA)26Sor locus. Expression is enhanced by the presence of a CAG promoter. Following Cre-mediated removal of the floxed STOP cassette, these mice can be used in optogenetic studies for rapid in vivo activation of excitable cells by illumination with blue light (450-490 nm). Allen Institute 012569
B6;129-Gt(ROSA)26Sortm1(COP4*H134R/*E123T,tdTomato)Gfng/J A targeting vector containing the CAG promoter, a loxP site flanked STOP fragment and pGK-NEO-pA cassette, 2 copies of channelrhodopsin-2 with E123T mutation (ChETA variant) and the H134R mutation, P2A-tdTomato variant of Enhanced Red Fluorescent Protein, and WPRE (Woodchuck Hepatitis Virus (WHP) Posttranscriptional Regulatory Element) sequence to enhance expression level, was inserted into the Gt(ROSA)26Sor locus. Guoping Feng 017455
VChR1
B6;SJL-Tg(Thy1-COP3/EYFP)1Gfng/J This line (founder line 1) has the expression of VChR1::YFP directed to neural cells by the murine thymus cell antigen 1 (Thy1) promoter region. Guoping Feng 012341
B6.SJL-Tg(Thy1-COP3/EYFP)4Gfng/J This line (founder line 4) has the expression of VChR1::YFP directed to neural cells by the murine thymus cell antigen 1 (Thy1) promoter region. Guoping Feng 012344
B6;SJL-Tg(Thy1-COP3/EYFP)8Gfng/J This line (founder line 8) has the expression of VChR1::YFP directed to neural cells by the murine thymus cell antigen 1 (Thy1) promoter region. Guoping Feng 012348

Links

References

Error fetching PMID 18552201:
Error fetching PMID 14615590:
Error fetching PMID 16116447:
Error fetching PMID 16306259:
Error fetching PMID 16990810:
Error fetching PMID 12089443:
Error fetching PMID 19079251:
Error fetching PMID 20081849:
Error fetching PMID 20621963:
Error fetching PMID 19254539:
Error fetching PMID 20886118:
Error fetching PMID 19641026:
Error fetching PMID 21315256:
Error fetching PMID 18614669:
Error fetching PMID 21504945:
Error fetching PMID 21693637:
Error fetching PMID 21048938:
Error fetching PMID 19377470:
Error fetching PMID 18160630:
Error fetching PMID 21692661:
Error fetching PMID 21745635:
Error fetching PMID 22044280:
Error fetching PMID 21994381:
Error fetching PMID 11721006:
Error fetching PMID 21796121:
Error fetching PMID 22196724:
Error fetching PMID 19103605:
Error fetching PMID 22773861:
Error fetching PMID 22843694:
Error fetching PMID 20000562:
Error fetching PMID 21889442:
Error fetching PMID 19103605:
  1. Error fetching PMID 22773861: [Wong2012]
  2. Error fetching PMID 20081849: [Gunaydin2010]
  3. Error fetching PMID 19079251: [Berndt2009]
  4. Error fetching PMID 20000562: [Bamann2010]
  5. Error fetching PMID 21796121: [Yizhar2011b]
  6. Error fetching PMID 21889442: [Gradmann2011]
  7. Error fetching PMID 19103605: [Wang2009]
  8. Error fetching PMID 19103605: [Wang2009]
  9. Error fetching PMID 22044280: [Hou2011]
  10. Error fetching PMID 21693637: [Govorunova2011]
  11. Error fetching PMID 22196724: [Zhang2011]
  12. Error fetching PMID 21504945: [Berndt2011]
  13. Error fetching PMID 11721006: [Facciotti2001]
  14. Error fetching PMID 18552201: [Berthold2008]
  15. Error fetching PMID 12089443: [Nagel2002]
  16. Error fetching PMID 19641026: [Kianianmomeni2009]
  17. Error fetching PMID 19254539: [Lin2009]
  18. Error fetching PMID 22843694: [Prigge2012]
  19. Error fetching PMID 19377470: [Lewis2009]
  20. Error fetching PMID 18160630: [Gradinaru2007]
  21. Error fetching PMID 21048938: [Grub2010]
  22. Error fetching PMID 21994381: [Wu2011]
  23. Error fetching PMID 21745635: [Yizhar2011a]
  24. Error fetching PMID 20621963: [Lin2010]
  25. Error fetching PMID 21692661: [Fenno2011]
  26. Error fetching PMID 14615590: [Nagel2003]
  27. Error fetching PMID 16116447: [Boyden2005]
  28. Error fetching PMID 16306259: [Li2005]
  29. Error fetching PMID 16990810: [Zhang2006]
  30. Error fetching PMID 20886118: [Wen2010]
  31. Error fetching PMID 18614669: [Atasoy2008]
  32. Error fetching PMID 21315256: [Ren2011]
All Medline abstracts: PubMed HubMed

References (pmids) which crash the biblio extension:

  • #Zhang2008 pmid=18432196
  • #Hagglund2010 pmid=20081850
  • #Kleinlogel2011 pmid=21399632