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Phospholipase D Transduces Force to TREK-1 Channels in a Biological Membrane

E. Nicholas Petersen, Manasa Gudheti, Mahmud Arif Pavel, Keith R. Murphy, William W. Ja, Erik M. Jorgensen, View ORCID ProfileScott B. Hansen
doi: https://doi.org/10.1101/758896
E. Nicholas Petersen
1Departments of Molecular Medicine, The Scripps Research Institute, Scripps, Florida 33458, USA
4Scripps Research Skaggs Graduate School of Chemical and Biological Sciences, The Scripps Research Institute, Scripps, Florida 33458, USA
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Manasa Gudheti
5Department of Biology, Howard Hughes Medical Institute, University of Utah, Salt Lake City, UT 84112, USA
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Mahmud Arif Pavel
1Departments of Molecular Medicine, The Scripps Research Institute, Scripps, Florida 33458, USA
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Keith R. Murphy
2Department of Neuroscience, The Scripps Research Institute, Scripps, Florida 33458, USA
3Center on Aging, The Scripps Research Institute, Scripps, Florida 33458, USA
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William W. Ja
2Department of Neuroscience, The Scripps Research Institute, Scripps, Florida 33458, USA
3Center on Aging, The Scripps Research Institute, Scripps, Florida 33458, USA
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Erik M. Jorgensen
5Department of Biology, Howard Hughes Medical Institute, University of Utah, Salt Lake City, UT 84112, USA
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Scott B. Hansen
1Departments of Molecular Medicine, The Scripps Research Institute, Scripps, Florida 33458, USA
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  • ORCID record for Scott B. Hansen
  • For correspondence: shansen@scripps.edu
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Abstract

The transduction of force into a biological signal is critical to all living organisms. Recently, disruption of ordered lipids has emerged as an ‘atypical’ force sensor in biological membranes; however, disruption has yet to link with canonical channel mechanosensation. Here we show that forceinduced disruption and lipid mixing activates TWIK-related K+ channel (TREK-1), and that this activation is dependent on phospholipase D2 (PLD2). PLD2 transduces the force into a chemical signal phosphatidic acid (PA) that is then sensed by TREK-1 with a latency of <3 ms. TREK-1 then produces a mechanically induced change in membrane potential. Hence, in a biological membrane, we show the ordered lipid is the force sensor, PLD2 is a chemical transducer, and the ‘mechanosensitive’ ion channel TREK-1 is a downstream effector of mechanical transduction. Confirming this central role for PA singling in force transduction, genetic deletion of PLD decreases mechanosensitivity and pain thresholds in D. melanogaster.

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Posted September 05, 2019.
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Phospholipase D Transduces Force to TREK-1 Channels in a Biological Membrane
E. Nicholas Petersen, Manasa Gudheti, Mahmud Arif Pavel, Keith R. Murphy, William W. Ja, Erik M. Jorgensen, Scott B. Hansen
bioRxiv 758896; doi: https://doi.org/10.1101/758896
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Phospholipase D Transduces Force to TREK-1 Channels in a Biological Membrane
E. Nicholas Petersen, Manasa Gudheti, Mahmud Arif Pavel, Keith R. Murphy, William W. Ja, Erik M. Jorgensen, Scott B. Hansen
bioRxiv 758896; doi: https://doi.org/10.1101/758896

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