We are analyzing https://link.springer.com/article/10.1007/s11068-008-9027-6.

Title:
eNpHR: a Natronomonas halorhodopsin enhanced for optogenetic applications | Brain Cell Biology
Description:
Temporally precise inhibition of distinct cell types in the intact nervous system has been enabled by the microbial halorhodopsin NpHR, a fast light-activated electrogenic Cl− pump. While neurons can be optically hyperpolarized and inhibited from firing action potentials at moderate NpHR expression levels, we have encountered challenges with pushing expression to extremely high levels, including apparent intracellular accumulations. We therefore sought to molecularly engineer NpHR to achieve strong expression without these cellular side effects. We found that high expression correlated with endoplasmic reticulum (ER) accumulation, and that under these conditions NpHR colocalized with ER proteins containing the KDEL ER retention sequence. We screened a number of different putative modulators of membrane trafficking and identified a combination of two motifs, an N-terminal signal peptide and a C-terminal ER export sequence, that markedly promoted membrane localization and ER export defined by confocal microscopy and whole-cell patch clamp. The modified NpHR displayed increased peak photocurrent in the absence of aggregations or toxicity, and potent optical inhibition was observed not only in vitro but also in vivo with thalamic single-unit recording. The new enhanced NpHR (eNpHR) allows safe, high-level expression in mammalian neurons, without toxicity and with augmented inhibitory function, in vitro and in vivo.
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Keywords {🔍}

nphr, enphr, article, google, scholar, pubmed, cas, expression, zhang, neurons, cell, vivo, deisseroth, export, fig, membrane, optical, neural, gradinaru, levels, high, aggregates, proteins, light, brain, confocal, surface, neurosci, signal, activity, chr, yellow, photocurrents, hippocampal, construct, injection, halorhodopsin, access, localization, mammalian, mice, nagel, control, cells, protein, signals, open, found, cterminal, vitro,

Topics {✒️}

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Schema {🗺️}

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         headline:eNpHR: a Natronomonas halorhodopsin enhanced for optogenetic applications
         description:Temporally precise inhibition of distinct cell types in the intact nervous system has been enabled by the microbial halorhodopsin NpHR, a fast light-activated electrogenic Cl− pump. While neurons can be optically hyperpolarized and inhibited from firing action potentials at moderate NpHR expression levels, we have encountered challenges with pushing expression to extremely high levels, including apparent intracellular accumulations. We therefore sought to molecularly engineer NpHR to achieve strong expression without these cellular side effects. We found that high expression correlated with endoplasmic reticulum (ER) accumulation, and that under these conditions NpHR colocalized with ER proteins containing the KDEL ER retention sequence. We screened a number of different putative modulators of membrane trafficking and identified a combination of two motifs, an N-terminal signal peptide and a C-terminal ER export sequence, that markedly promoted membrane localization and ER export defined by confocal microscopy and whole-cell patch clamp. The modified NpHR displayed increased peak photocurrent in the absence of aggregations or toxicity, and potent optical inhibition was observed not only in vitro but also in vivo with thalamic single-unit recording. The new enhanced NpHR (eNpHR) allows safe, high-level expression in mammalian neurons, without toxicity and with augmented inhibitory function, in vitro and in vivo.
         datePublished:2008-08-02T00:00:00Z
         dateModified:2008-08-02T00:00:00Z
         pageStart:129
         pageEnd:139
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            Adult Mouse Hippocampus
            Neurosciences
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            Cell Biology
            Life Sciences
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            Biological Microscopy
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      headline:eNpHR: a Natronomonas halorhodopsin enhanced for optogenetic applications
      description:Temporally precise inhibition of distinct cell types in the intact nervous system has been enabled by the microbial halorhodopsin NpHR, a fast light-activated electrogenic Cl− pump. While neurons can be optically hyperpolarized and inhibited from firing action potentials at moderate NpHR expression levels, we have encountered challenges with pushing expression to extremely high levels, including apparent intracellular accumulations. We therefore sought to molecularly engineer NpHR to achieve strong expression without these cellular side effects. We found that high expression correlated with endoplasmic reticulum (ER) accumulation, and that under these conditions NpHR colocalized with ER proteins containing the KDEL ER retention sequence. We screened a number of different putative modulators of membrane trafficking and identified a combination of two motifs, an N-terminal signal peptide and a C-terminal ER export sequence, that markedly promoted membrane localization and ER export defined by confocal microscopy and whole-cell patch clamp. The modified NpHR displayed increased peak photocurrent in the absence of aggregations or toxicity, and potent optical inhibition was observed not only in vitro but also in vivo with thalamic single-unit recording. The new enhanced NpHR (eNpHR) allows safe, high-level expression in mammalian neurons, without toxicity and with augmented inhibitory function, in vitro and in vivo.
      datePublished:2008-08-02T00:00:00Z
      dateModified:2008-08-02T00:00:00Z
      pageStart:129
      pageEnd:139
      license:https://creativecommons.org/licenses/by-nc/2.0
      sameAs:https://doi.org/10.1007/s11068-008-9027-6
      keywords:
         FUDR
         Endoplasmic Reticulum Retention
         Mammalian Neuron
         Endoplasmic Reticulum Export
         Adult Mouse Hippocampus
         Neurosciences
         Neurobiology
         Cell Biology
         Life Sciences
         general
         Biological Microscopy
         Developmental Biology
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            address:
               name:Program in Neuroscience, Stanford University, Stanford, USA
               type:PostalAddress
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      affiliation:
            name:Stanford University
            address:
               name:Department of Bioengineering, Stanford University, Stanford, USA
               type:PostalAddress
            type:Organization
      name:Karl Deisseroth
      affiliation:
            name:Stanford University
            address:
               name:Department of Bioengineering, Stanford University, Stanford, USA
               type:PostalAddress
            type:Organization
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            address:
               name:Department of Psychiatry and Behavioral Sciences, Stanford University, Stanford, USA
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      name:Department of Psychiatry and Behavioral Sciences, Stanford University, Stanford, USA

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