Identification of a Membrane-targeting Domain of the Transient Receptor Potential Canonical (TRPC)4 Channel Unrelated to Its Formation of a Tetrameric Structure

Myeong, Jongyun; Kwak, Misun; Hong, Chansik; Jeon, Ju Hong; So, Insuk

doi:10.1074/jbc.m114.584649

Cited by 14 publications

(8 citation statements)

References 55 publications

(58 reference statements)

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“…The I-V curve showed a typical doubly rectifying shape, consistent with previous reports (Fig. 3B) [2324252627]. The current at -60 mV increased from -10.…”

Section: Resultssupporting

confidence: 91%

Calcium permeability of transient receptor potential canonical (TRPC) 4 channels measured by TRPC4-GCaMP6s

Myeong

Yang

et al. 2017

Korean J Physiol Pharmacol

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Conflicting evidence has been obtained regarding whether transient receptor potential cation channels (TRPC) are store-operated channels (SOCs) or receptor-operated channels (ROCs). Moreover, the Ca/Na permeability ratio differs depending on whether the current-voltage (I-V) curve has a doubly rectifying shape or inward rectifying shape. To investigate the calcium permeability of TRPC4 channels, we attached GCaMP6s to TRPC4 and simultaneously measured the current and calcium signals. A TRPC4 specific activator, (–)-englerin A, induced both current and calcium fluorescence with the similar time course. Muscarinic receptor stimulator, carbachol, also induced both current and calcium fluorescence with the similar time course. By forming heteromers with TRPC4, TRPC1 significantly reduced the inward current with outward rectifying I-V curve, which also caused the decrease of calcium fluorescence intensity. These results suggest that GCaMP6s attached to TRPC4 can detect slight calcium changes near TRPC4 channels. Consequently, TRPC4-GCaMP6s can be a useful tool for testing the calcium permeability of TRPC4 channels.

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“…The I-V curve showed a typical doubly rectifying shape, consistent with previous reports (Fig. 3B) [2324252627]. The current at -60 mV increased from -10.…”

Section: Resultssupporting

confidence: 91%

Calcium permeability of transient receptor potential canonical (TRPC) 4 channels measured by TRPC4-GCaMP6s

Myeong

Yang

et al. 2017

Korean J Physiol Pharmacol

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“…In this context, TRP tetramerization involves transmembrane segments (Hellwig et al, 2005), ARD (Arniges et al, 2006;Erler et al, 2004;Hellwig et al, 2005), and different regions of the N tails (Chang et al, 2004;Myeong et al, 2014;Pertusa et al, 2014) and C tails (Becker et al, 2008;Erler et al, 2006;Hellwig et al, 2005;Lei et al, 2013;Zhang et al, 2011), including the TRP box (GarciaSanz et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Interaction between the Linker, Pre-S1, and TRP Domains Determines Folding, Assembly, and Trafficking of TRPV Channels

et al. 2015

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Functional transient receptor potential (TRP) channels result from the assembly of four subunits. Here, we show an interaction between the pre-S1, TRP, and the ankyrin repeat domain (ARD)-S1 linker domains of TRPV1 and TRPV4 that is essential for proper channel assembly. Neutralization of TRPV4 pre-S1 K462 resulted in protein retention in the ER, defective glycosylation and trafficking, and unresponsiveness to TRPV4-activating stimuli. Similar results were obtained with the equivalent mutation in TRPV1 pre-S1. Molecular dynamics simulations revealed that TRPV4-K462 generated an alternating hydrogen network with E745 (TRP box) and D425 (pre-S1 linker), and that K462Q mutation affected subunit folding. Consistently, single TRPV4-E745A or TRPV4-D425A mutations moderately affected TRPV4 biogenesis while double TRPV4-D425A/E745A mutation resumed the TRPV4-K462Q phenotype. Thus, the interaction between pre-S1, TRP, and linker domains is mandatory to generate a structural conformation that allows the contacts between adjacent subunits to promote correct assembly and trafficking to the plasma membrane.

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“…In addition to prestin, Ibsen and colleagues demonstrated that the mechanosensitive ion channel, TRP-4, is required for ultrasound-mediated mechanical stimulation and can modify animal behaviour in the presence of MBs 16 . To test whether TRP-4 can act as an ultrasound-responsive protein, we transfected HEK293T cells with two members of the mammalian TRPC4 family including human TRPC4α (hTRPC4α) use TRPC4β (mTRPC4β) 27,28 . The calcium response of cells expressing hTRPC4α or mTRPC4β tagged with CFP upon FUS stimulation of different frequencies was examined and quantified.…”

Section: Resultsmentioning

confidence: 99%

Sonogenetic modulation of cellular activities using an engineered auditory-sensing protein

Huang

Fan

Hsu

et al. 2019

Preprint

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24Biomolecules that respond to different external stimuli enable the remote control of genetically 25 modified cells. Chemogenetics and optogenetics, two tools that can control cellular activities 26 via synthetic chemicals or photons, respectively, have been widely used to elucidate underlying 27 physiological processes. These methods are, however, very invasive, have poor penetrability, 28 or low spatiotemporal precision, attributes that hinder their use in therapeutic applications. We 29 report herein a sonogenetic approach that can manipulate target cell activities by focused 30 ultrasound stimulation. This system requires an ultrasound-responsive protein derived from an 31 engineered auditory-sensing protein prestin. Heterogeneous expression of mouse prestin 32 containing two parallel amino acid substitutions, N7T and N308S, that frequently exist in 33 prestins from echolocating species endowed transfected mammalian cells with the ability to 34 sense ultrasound. An ultrasound pulse of low frequency and low pressure efficiently evoked 35 cellular calcium responses after transfecting with prestin(N7T, N308S). Moreover, pulsed 36 ultrasound can also non-invasively stimulate target neurons expressing prestin(N7T, N308S) 37 in deep regions of mice brains. Our study delineates how an engineered auditory-sensing 38 protein can cause mammalian cells to sense ultrasound stimulation. Moreover, owing to the 39 great penetration of low-frequency ultrasound (~400 mm in depth), our sonogenetic tools will 40 serve as new strategies for non-invasive therapy in deep tissues of large animals like primates. 41 42 43 44 45 46

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Identification of a Membrane-targeting Domain of the Transient Receptor Potential Canonical (TRPC)4 Channel Unrelated to Its Formation of a Tetrameric Structure

Cited by 14 publications

References 55 publications

Calcium permeability of transient receptor potential canonical (TRPC) 4 channels measured by TRPC4-GCaMP6s

Calcium permeability of transient receptor potential canonical (TRPC) 4 channels measured by TRPC4-GCaMP6s

Interaction between the Linker, Pre-S1, and TRP Domains Determines Folding, Assembly, and Trafficking of TRPV Channels

Sonogenetic modulation of cellular activities using an engineered auditory-sensing protein

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