Photochemical control of endogenous ion channels and cellular excitability

Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels th...

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Published inNature methods Vol. 5; no. 4; pp. 331 - 338
Main Authors Trauner, Dirk, Kristan, William B, Gaudry, Quentin, Borges, Katharine, Otis, Thomas S, Dunn, Timothy W, Karakossian, Movses H, Kramer, Richard H, Fortin, Doris L, Banghart, Matthew R, Wagenaar, Daniel A
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.04.2008
Nature Publishing Group
Subjects
Action Potentials - radiation effects
Affinity Labels - chemistry
Animals
Azo Compounds - chemistry
Bioinformatics
Biological Microscopy
Biological Techniques
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
Calcium
Cells
Cells, Cultured
Cerebellum - cytology
Cerebellum - metabolism
Cerebellum - radiation effects
Gene expression
Genes
Hippocampus - cytology
Hippocampus - metabolism
Hippocampus - radiation effects
Hirudinea
Ion Channel Gating - radiation effects
Ion channels
Ions
Isomerization
Leeches
Life Sciences
Methods
Neurons - metabolism
Neurons - radiation effects
Optical properties
Photic Stimulation
Photochemicals
Photochemistry
Physiological aspects
Potassium Channels - metabolism
Proteomics
Quaternary Ammonium Compounds - chemistry
Rats
Wavelengths
United States
Online AccessGet full text

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Abstract Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels that does not rely on exogenous gene expression. The method uses a synthetic photoisomerizable small molecule, or photoswitchable affinity label (PAL), that specifically targets K + channels. PALs contain a reactive electrophile, enabling covalent attachment of the photoswitch to naturally occurring nucleophiles in K + channels. Ion flow through PAL-modified channels is turned on or off by photoisomerizing PAL with different wavelengths of light. We showed that PAL treatment confers light sensitivity onto endogenous K + channels in isolated rat neurons and in intact neural structures from rat and leech, allowing rapid optical regulation of excitability without genetic modification.
AbstractList Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels that does not rely on exogenous gene expression. The method uses a synthetic photoisomerizable small molecule, or photoswitchable affinity label (PAL), that specifically targets K + channels. PALs contain a reactive electrophile, enabling covalent attachment of the photoswitch to naturally occurring nucleophiles in K + channels. Ion flow through PAL-modified channels is turned on or off by photoisomerizing PAL with different wavelengths of light. We showed that PAL treatment confers light sensitivity onto endogenous K + channels in isolated rat neurons and in intact neural structures from rat and leech, allowing rapid optical regulation of excitability without genetic modification. [PUBLICATION ABSTRACT
Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels that does not rely on exogenous gene expression. The method uses a synthetic photoisomerizable small molecule, or photoswitchable affinity label (PAL), that specifically targets K + channels. PALs contain a reactive electrophile, enabling covalent attachment of the photoswitch to naturally occurring nucleophiles in K + channels. Ion flow through PAL-modified channels is turned on or off by photoisomerizing PAL with different wavelengths of light. We showed that PAL treatment confers light sensitivity onto endogenous K + channels in isolated rat neurons and in intact neural structures from rat and leech, allowing rapid optical regulation of excitability without genetic modification.
Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels that does not rely on exogenous gene expression. The method uses a synthetic photoisomerizable small molecule, or photoswitchable affinity label (PAL), that specifically targets K+ channels. PALs contain a reactive electrophile, enabling covalent attachment of the photoswitch to naturally occurring nucleophiles in K+ channels. Ion flow through PAL-modified channels is turned on or off by photoisomerizing PAL with different wavelengths of light. We showed that PAL treatment confers light sensitivity onto endogenous K+ channels in isolated rat neurons and in intact neural structures from rat and leech, allowing rapid optical regulation of excitability without genetic modification.
Light-activated ion channels provide a precise and non-invasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels that does not rely on exogenous gene expression. The method utilizes a synthetic photoisomerizable small molecule, or Photoswitchable Affinity Label (PAL), that specifically targets K + channels. PALs contain a reactive electrophile, enabling covalent attachment of the photoswitch to naturally occurring nucleophiles in K + channels. Ion flow through PAL-modified channels is turned on or off by photoisomerizing PAL with different wavelengths of light. We show that PAL treatment confers light sensitivity onto endogenous K + channels in isolated neurons and intact neural structures, allowing rapid optical regulation of excitability without genetic modification.
Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels must first be delivered and expressed in target cells. Here we describe a method for bestowing light sensitivity onto endogenous ion channels that does not rely on exogenous gene expression. The method uses a synthetic photoisomerizable small molecule, or photoswitchable affinity label (PAL), that specifically targets K super(+) channels. PALs contain a reactive electrophile, enabling covalent attachment of the photoswitch to naturally occurring nucleophiles in K super(+) channels. Ion flow through PAL-modified channels is turned on or off by photoisomerizing PAL with different wavelengths of light. We showed that PAL treatment confers light sensitivity onto endogenous K super(+) channels in isolated rat neurons and in intact neural structures from rat and leech, allowing rapid optical regulation of excitability without genetic modification.
Audience Academic
Author Wagenaar, Daniel A
Karakossian, Movses H
Kramer, Richard H
Otis, Thomas S
Trauner, Dirk
Fortin, Doris L
Dunn, Timothy W
Banghart, Matthew R
Gaudry, Quentin
Borges, Katharine
Kristan, William B
AuthorAffiliation 3 Department of Biology, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92037-0357
1 Department of Molecular and Cell Biology, University of California Berkeley, 121 Life Sciences Addition, Berkeley, CA 94720-3200
4 Department of Neurobiology, University of California, Los Angeles, 63-314 CHS Box 951763, Los Angeles, CA 90095-1763
2 Department of Chemistry, University of California Berkeley, Latimer Hall, Berkeley, CA 94720-1460
AuthorAffiliation_xml – name: 1 Department of Molecular and Cell Biology, University of California Berkeley, 121 Life Sciences Addition, Berkeley, CA 94720-3200
– name: 2 Department of Chemistry, University of California Berkeley, Latimer Hall, Berkeley, CA 94720-1460
– name: 4 Department of Neurobiology, University of California, Los Angeles, 63-314 CHS Box 951763, Los Angeles, CA 90095-1763
– name: 3 Department of Biology, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92037-0357
Author_xml – givenname: Dirk
  surname: Trauner
  fullname: Trauner, Dirk
  organization: Department of Chemistry, University of California Berkeley
– givenname: William B
  surname: Kristan
  fullname: Kristan, William B
  organization: Department of Biology, University of California San Diego
– givenname: Quentin
  surname: Gaudry
  fullname: Gaudry, Quentin
  organization: Department of Biology, University of California San Diego
– givenname: Katharine
  surname: Borges
  fullname: Borges, Katharine
  organization: Department of Molecular and Cell Biology, University of California Berkeley, 121 Life Sciences Addition
– givenname: Thomas S
  surname: Otis
  fullname: Otis, Thomas S
  organization: Department of Neurobiology, University of California, Los Angeles, 63-314 CHS Box 951763
– givenname: Timothy W
  surname: Dunn
  fullname: Dunn, Timothy W
  organization: Department of Molecular and Cell Biology, University of California Berkeley, 121 Life Sciences Addition
– givenname: Movses H
  surname: Karakossian
  fullname: Karakossian, Movses H
  organization: Department of Neurobiology, University of California, Los Angeles, 63-314 CHS Box 951763
– givenname: Richard H
  surname: Kramer
  fullname: Kramer, Richard H
  organization: Department of Molecular and Cell Biology, University of California Berkeley, 121 Life Sciences Addition
– givenname: Doris L
  surname: Fortin
  fullname: Fortin, Doris L
  organization: Department of Molecular and Cell Biology, University of California Berkeley, 121 Life Sciences Addition
– givenname: Matthew R
  surname: Banghart
  fullname: Banghart, Matthew R
  organization: Department of Chemistry, University of California Berkeley
– givenname: Daniel A
  surname: Wagenaar
  fullname: Wagenaar, Daniel A
  organization: Department of Biology, University of California San Diego
BackLink https://www.ncbi.nlm.nih.gov/pubmed/18311146$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright Springer Nature America, Inc. 2008
COPYRIGHT 2008 Nature Publishing Group
Copyright Nature Publishing Group Apr 2008
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Snippet Light-activated ion channels provide a precise and noninvasive optical means for controlling action potential firing, but the genes encoding these channels...
Light-activated ion channels provide a precise and non-invasive optical means for controlling action potential firing, but the genes encoding these channels...
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crossref
pubmed
springer
nature
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StartPage 331
SubjectTerms Action Potentials - radiation effects
Affinity Labels - chemistry
Animals
Azo Compounds - chemistry
Bioinformatics
Biological Microscopy
Biological Techniques
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
Calcium
Cells
Cells, Cultured
Cerebellum - cytology
Cerebellum - metabolism
Cerebellum - radiation effects
Gene expression
Genes
Hippocampus - cytology
Hippocampus - metabolism
Hippocampus - radiation effects
Hirudinea
Ion Channel Gating - radiation effects
Ion channels
Ions
Isomerization
Leeches
Life Sciences
Methods
Neurons - metabolism
Neurons - radiation effects
Optical properties
Photic Stimulation
Photochemicals
Photochemistry
Physiological aspects
Potassium Channels - metabolism
Proteomics
Quaternary Ammonium Compounds - chemistry
Rats
Wavelengths
Title Photochemical control of endogenous ion channels and cellular excitability
URI http://dx.doi.org/10.1038/nmeth.1187
https://link.springer.com/article/10.1038/nmeth.1187
https://www.ncbi.nlm.nih.gov/pubmed/18311146
https://www.proquest.com/docview/223235528
https://search.proquest.com/docview/20866852
https://search.proquest.com/docview/70453967
https://pubmed.ncbi.nlm.nih.gov/PMC2760097
Volume 5
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