International Union of Basic and Clinical Pharmacology. LXXVI. Current Progress in the Mammalian TRP Ion Channel Family

Wu, Long Jun; Sweet, Tara Beth; Clapham, David E.

doi:10.1124/pr.110.002725

Cited by 520 publications

(527 citation statements)

References 400 publications

(446 reference statements)

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“…In contrast, carbachol application was sufficient to induce the translocation of the GFP-tagged pleckstrin homology domain of PLCδ1 [GFP-PLCδ1-PH, a PI(4,5)P 2 probe (5)] from plasma membrane to cytosol within seconds (Fig. S5), and readily activated receptor-operated hTRPC6 channels (25) in HM1 cells (Fig. S5).…”

Section: Resultsmentioning

confidence: 99%

Phosphoinositide isoforms determine compartment-specific ion channel activity

Zhang

2012

Proc. Natl. Acad. Sci. U.S.A.

139

140

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Phosphoinositides serve as address labels for recruiting peripheral cytoplasmic proteins to specific subcellular compartments, and as endogenous factors for modulating the activity of integral membrane proteins. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P 2 ) is a plasma-membrane (PM)-specific phosphoinositide and a positive cofactor required for the activity of most PM channels and transporters. This requirement for phosphoinositide cofactors has been proposed to prevent PM channel/transporter activity during passage through the biosynthetic/secretory and endocytic pathways. To determine whether intracellularly localized channels are similarly "inactivated" at the PM, we studied PIP 2 modulation of intracellular TRPML1 channels. TRPML1 channels are primarily localized in lysosomes, but can also be detected temporarily in the PM upon lysosomal exocytosis. By directly patch-clamping isolated lysosomes, we previously found that lysosomal, but not PMlocalized, TRPML1 is active with PI(3,5)P 2 , a lysosome-specific PIP 2 , as the underlying positive cofactor. Here we found that "silent" PM-localized TRPML1 could be activated by depleting PI(4,5)P 2 levels and/or by adding PI(3,5)P 2 to inside-out membrane patches. Unlike PM channels, surface-expressed TRPML1 underwent a unique and characteristic run-up upon patch excision, and was potently inhibited by a low micromolar concentration of PI(4,5)P 2 . Conversely, depletion of PI(4,5)P 2 by either depolarization-induced activation or chemically induced translocation of 5′-phosphatase potentiated whole-cell TRPML1 currents. PI(3,5)P 2 activation and PI(4,5)P 2 inhibition of TRPML1 were mediated by distinct basic amino acid residues in a common PIP 2 -interacting domain. Thus, PI(4,5)P 2 may serve as a negative cofactor for intracellular channels such as TRPML1. Based on these results, we propose that phosphoinositide regulation sets compartment-specific activity codes for membrane channels and transporters.TRP channel | mucolipin

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Section: Resultsmentioning

confidence: 99%

Phosphoinositide isoforms determine compartment-specific ion channel activity

Zhang

2012

Proc. Natl. Acad. Sci. U.S.A.

139

140

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“…1C). We found that the UVR photocurrent is outwardly rectifying and has a reversal potential near 0 mV, a current-voltage relationship consistent with many TRP channels (18).…”

mentioning

confidence: 81%

UV light phototransduction activates transient receptor potential A1 ion channels in human melanocytes

Bellono

Kammel

Zimmerman

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

129

139

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Human skin is constantly exposed to solar ultraviolet radiation (UVR), the most prevalent environmental carcinogen. Humans have the unique ability among mammals to respond to UVR by increasing their skin pigmentation, a protective process driven by melanin synthesis in epidermal melanocytes. The molecular mechanisms used by melanocytes to detect and respond to longwavelength UVR (UVA) are not well understood. We recently identified a UVA phototransduction pathway in melanocytes that is mediated by G protein-coupled receptors and leads to rapid calcium mobilization. Here we report that in human epidermal melanocytes physiological doses of UVR activate a retinal-dependent current mediated by transient receptor potential A1 (TRPA1) ion channels. The TRPA1 photocurrent is UVA-specific and requires G protein and phospholipase C signaling, thus contributing to UVAinduced calcium responses to mediate downstream cellular effects and providing evidence for TRPA1 function in mammalian phototransduction. Remarkably, TRPA1 activation is required for the UVR-induced and retinal-dependent early increase in cellular melanin. Our results show that TRPA1 is essential for a unique extraocular phototransduction pathway in human melanocytes that is activated by physiological doses of UVR and results in early melanin synthesis.

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“…Gating of TRP channels is controlled by a broad range of physical and chemical stimuli that vary between and within TRP families. Common elements among TRP channels are their Ca 2+ permeability and potentiation by receptors coupled to G q (reviewed by Wu et al 2010). Members of the TRPC family (C for Bclassic^or Bcanonical^) are expressed in the brain where they participate in synaptic functions mediated by mGlu receptors (reviewed by Hartmann and Konnerth 2015).…”

Section: Trpc Channelsmentioning

confidence: 99%

Control of neuronal excitability by Group I metabotropic glutamate receptors

Amb

Jds

et al. 2017

Biophys Rev

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Metabotropic glutamate (mGlu) receptors couple through G proteins to regulate a large number of cell functions. Eight mGlu receptor isoforms have been cloned and classified into three Groups based on sequence, signal transduction mechanisms and pharmacology. This review will focus on Group I mGlu receptors, comprising the isoforms mGlu 1 and mGlu 5 . Activation of these receptors initiates both G protein-dependent and -independent signal transduction pathways. The G-protein-dependent pathway involves mainly Gα q , which can activate PLCβ, leading initially to the formation of IP 3 and diacylglycerol. IP 3 can release Ca 2+ from cellular stores resulting in activation of Ca 2+ -dependent ion channels. Intracellular Ca 2+ , together with diacylglycerol, activates PKC, which has many protein targets, including ion channels. Thus, activation of the G-protein-dependent pathway affects cellular excitability though several different effectors. In parallel, G protein-independent pathways lead to activation of non-selective cationic currents and metabotropic synaptic currents and potentials. Here, we provide a survey of the membrane transport proteins responsible for these electrical effects of Group I metabotropic glutamate receptors.

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International Union of Basic and Clinical Pharmacology. LXXVI. Current Progress in the Mammalian TRP Ion Channel Family

Cited by 520 publications

References 400 publications

Phosphoinositide isoforms determine compartment-specific ion channel activity

Phosphoinositide isoforms determine compartment-specific ion channel activity

UV light phototransduction activates transient receptor potential A1 ion channels in human melanocytes

Control of neuronal excitability by Group I metabotropic glutamate receptors

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