Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila
A major gap in our understanding of sensation is how a single sensory neuron can differentially respond to a multitude of different stimuli (polymodality), such as propio- or nocisensation. The prevailing hypothesis is that different stimuli are transduced through ion channels with diverse propertie...
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Format: | Article |
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Elsevier
2014-11-01
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Series: | Cell Reports |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124714009036 |
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author | David A. Gorczyca Susan Younger Shan Meltzer Sung Eun Kim Li Cheng Wei Song Hye Young Lee Lily Yeh Jan Yuh Nung Jan |
author_facet | David A. Gorczyca Susan Younger Shan Meltzer Sung Eun Kim Li Cheng Wei Song Hye Young Lee Lily Yeh Jan Yuh Nung Jan |
author_sort | David A. Gorczyca |
collection | DOAJ |
description | A major gap in our understanding of sensation is how a single sensory neuron can differentially respond to a multitude of different stimuli (polymodality), such as propio- or nocisensation. The prevailing hypothesis is that different stimuli are transduced through ion channels with diverse properties and subunit composition. In a screen for ion channel genes expressed in polymodal nociceptive neurons, we identified Ppk26, a member of the trimeric degenerin/epithelial sodium channel (DEG/ENaC) family, as being necessary for proper locomotion behavior in Drosophila larvae in a mutually dependent fashion with coexpressed Ppk1, another member of the same family. Mutants lacking Ppk1 and Ppk26 were defective in mechanical, but not thermal, nociception behavior. Mutants of Piezo, a channel involved in mechanical nociception in the same neurons, did not show a defect in locomotion, suggesting distinct molecular machinery for mediating locomotor feedback and mechanical nociception. |
first_indexed | 2024-12-13T00:45:15Z |
format | Article |
id | doaj.art-72503fc52ae841159fcb726e6e3c7108 |
institution | Directory Open Access Journal |
issn | 2211-1247 |
language | English |
last_indexed | 2024-12-13T00:45:15Z |
publishDate | 2014-11-01 |
publisher | Elsevier |
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series | Cell Reports |
spelling | doaj.art-72503fc52ae841159fcb726e6e3c71082022-12-22T00:05:03ZengElsevierCell Reports2211-12472014-11-01941446145810.1016/j.celrep.2014.10.034Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in DrosophilaDavid A. Gorczyca0Susan Younger1Shan Meltzer2Sung Eun Kim3Li Cheng4Wei Song5Hye Young Lee6Lily Yeh Jan7Yuh Nung Jan8Neuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USANeuroscience Graduate Program, University of California San Francisco, San Francisco, CA 94158, USAA major gap in our understanding of sensation is how a single sensory neuron can differentially respond to a multitude of different stimuli (polymodality), such as propio- or nocisensation. The prevailing hypothesis is that different stimuli are transduced through ion channels with diverse properties and subunit composition. In a screen for ion channel genes expressed in polymodal nociceptive neurons, we identified Ppk26, a member of the trimeric degenerin/epithelial sodium channel (DEG/ENaC) family, as being necessary for proper locomotion behavior in Drosophila larvae in a mutually dependent fashion with coexpressed Ppk1, another member of the same family. Mutants lacking Ppk1 and Ppk26 were defective in mechanical, but not thermal, nociception behavior. Mutants of Piezo, a channel involved in mechanical nociception in the same neurons, did not show a defect in locomotion, suggesting distinct molecular machinery for mediating locomotor feedback and mechanical nociception.http://www.sciencedirect.com/science/article/pii/S2211124714009036 |
spellingShingle | David A. Gorczyca Susan Younger Shan Meltzer Sung Eun Kim Li Cheng Wei Song Hye Young Lee Lily Yeh Jan Yuh Nung Jan Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila Cell Reports |
title | Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila |
title_full | Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila |
title_fullStr | Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila |
title_full_unstemmed | Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila |
title_short | Identification of Ppk26, a DEG/ENaC Channel Functioning with Ppk1 in a Mutually Dependent Manner to Guide Locomotion Behavior in Drosophila |
title_sort | identification of ppk26 a deg enac channel functioning with ppk1 in a mutually dependent manner to guide locomotion behavior in drosophila |
url | http://www.sciencedirect.com/science/article/pii/S2211124714009036 |
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