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Lipid rafts transduce force to TREK‐1 channels via phospholipase D
Author(s) -
Petersen E. Nicholas,
Gudheti Manasa,
Pavel Mahmud Arif,
Murphy Keith R,
Ja William,
Jorgensen Erik,
Hansen Scott
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.797.6
Subject(s) - mechanosensitive channels , mechanosensation , pld2 , phosphatidic acid , microbiology and biotechnology , ion channel , signal transduction , transduction (biophysics) , phospholipase c , chemistry , mechanotransduction , biophysics , biology , neuroscience , membrane , biochemistry , phospholipid , receptor
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. We show here that force‐induced disruption and lipid mixing activates TREK‐1. This activation is dependent on PLD2 which transduces the force into the chemical signal phosphatidic acid that is then sensed by TREK‐1 with a latency of <3 ms. TREK‐1 then produces a mechanically induced change in membrane potential. These experiments establish the ordered lipid as the force sensor, PLD2 as the primary chemical transducer, and the ‘mechanosensitive’ ion channel TREK‐1 as a downstream effector of mechanical transduction. Confirming a central role for PA singling in force transduction, genetic deletion of PLD2 decreases mechanosensitivity and pain thresholds in D. melanogaster . Support or Funding Information NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE NATIONAL INSTITUTE OF AGEING HOWARD HUGHES MEDICAL INSTITUTE This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .