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        Sensing of lysophospholipids by TRPC5 calcium channel

        Author
        Flemming, Philippa K
        Dedman, Alexandra M
        Xu, Shang-Zhong
        Li, Jing
        Zeng, Fanning
        Naylor, Jacqueline
        Benham, Christopher D
        Bateson, Alan N
        Muraki, Katsuhiko
        Beech, David J
        Attention
        2299/3482
        Abstract
        TRPC calcium channels are emerging as a ubiquitous feature of vertebrate cells, but understanding of them is hampered by limited knowledge of the mechanisms of activation and identity of endogenous regulators. We have revealed that one of the TRPC channels, TRPC5, is strongly activated by common endogenous lysophospholipids including lysophosphatidylcholine (LPC) but, by contrast, not arachidonic acid. Although TRPC5 was stimulated by agonists at G-protein-coupled receptors, TRPC5 activation by LPC occurred downstream and independently of G-protein signaling. The effect was not due to the generation of reactive oxygen species or because of a detergent effect of LPC. LPC activated TRPC5 when applied to excised membrane patches and thus has a relatively direct action on the channel structure, either because of a phospholipid binding site on the channel or because of sensitivity of the channel to perturbation of the bilayer by certain lipids. Activation showed dependence on side-chain length and the chemical head-group. The data revealed a previously unrecognized lysophospholipid-sensing capability of TRPC5 that confers the property of a lipid ionotropic receptor.
        Publication date
        2006
        Published in
        Journal of Biological Chemistry
        Published version
        https://doi.org/10.1074/jbc.M510301200
        Other links
        http://hdl.handle.net/2299/3482
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