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Kinetic disruption of lipid rafts is a mechanosensor for phospholipase D

Petersen, E. Nicholas, Chung, Hae-Won, Nayebosadri, Arman, Hansen, Scott B.·2016·Nature Communications
DOI 10.1038/ncomms13873PMC PMC5171650
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Abstract

The sensing of physical force, mechanosensation, underlies two of five human senses—touch and hearing. How transduction of force in a membrane occurs remains unclear. We asked if a biological membrane could employ kinetic energy to transduce a signal absent tension. Here we show that lipid rafts are dynamic compartments that inactivate the signalling enzyme phospholipase D2 (PLD2) by sequestering the enzyme from its substrate. Mechanical disruption of the lipid rafts activates PLD2 by mixing the enzyme with its substrate to produce the signalling lipid phosphatidic acid (PA). We calculate a latency time of <650 μs for PLD activation by mixing. Our results establish a fast, non-tension mechanism for mechanotransduction where disruption of ordered lipids initiates a mechanosensitive signal for cell growth through mechanical mixing.

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  • GM1 domains are separate from phosphatidylinositol 4,5 bisphosphate domains, which are polyunsaturated and cholesterol independent.

    “These GM1 domains are separate from phosphatidylinositol 4,5 bisphosphate domains, which are polyunsaturated and cholesterol independent (18, 32, 33).”

    From Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterol (2021) · cites this paper as [18]

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Research works printed but not linked: 42

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Metadata

Authors
Petersen, E. N., Chung, H.-W., Nayebosadri, A., & Hansen, S. B.
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2016-12-15
Volume
7
Issue
1
ISSN
2041-1723
DOI
10.1038/ncomms13873
PMC
PMC5171650
Cited by
129
References
2
Language
en
Licence

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