Canonical Transient Receptor Potential (TRPC) 1 Acts as a Negative Regulator for Vanilloid TRPV6-mediated Ca2+ Influx

Schindl, Rainer; Fritsch, Reinhard; Jardín, Isaac; Frischauf, Irene; Kahr, Heike; Muik, Martin; Riedl, Maria Christine; Gröschner, Klaus; Romanin, Christoph

doi:10.1074/jbc.m112.400952

Cited by 46 publications

(33 citation statements)

References 52 publications

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“…Intriguingly, TRPV6 was found to coimmunoprecipitate with TRPC1 suggesting a role for the TRPC1 channel in TRPV6 trafficking and/or regulation. Indeed, it was recently shown that the TRPC1 channel may form heterotetramers with the TRPV6 channel and be a negative regulator of TRPV6 channel activity in the overexpression system in the HEK293 cell line (30). Together, these observations suggest a crucial role of Orai1/TRPC1-mediated SOCE in TRPV6 translocation.…”

Section: Discussionmentioning

confidence: 52%

TRPV6 calcium channel translocates to the plasma membrane via Orai1-mediated mechanism and controls cancer cell survival

Raphaël

Lehen’kyi

Vandenberghe

et al. 2014

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

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Transient receptor potential vanilloid subfamily member 6 (TRPV6) is a highly selective calcium channel that has been considered as a part of store-operated calcium entry (SOCE). Despite its first discovery in the early 2000s, the role of this channel in prostate cancer (PCa) remained, until now, obscure. Here we show that TRPV6 mediates calcium entry, which is highly increased in PCa due to the remodeling mechanism involving the translocation of the TRPV6 channel to the plasma membrane via the Orai1/TRPC1-mediated Ca 2+

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Section: Discussionmentioning

confidence: 52%

TRPV6 calcium channel translocates to the plasma membrane via Orai1-mediated mechanism and controls cancer cell survival

Raphaël

Lehen’kyi

Vandenberghe

et al. 2014

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

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“…An opposite (positive) effect on plasma membrane abundance of TRPV6 was demonstrated for WNK3 (Zhang et al, 2008c). It is noteworthy that TRPC1 might have an inhibitory effect on TRPV6 (Schindl et al, 2012).…”

Section: Trp Channels As Drug Targetsmentioning

confidence: 86%

Transient Receptor Potential Channels as Drug Targets: From the Science of Basic Research to the Art of Medicine

2014

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“…The interaction was mediated by the N-terminal ankyrin repeats of the two proteins and resulted in the reduction of TRPV6-mediated currents in transfected HEK293 cells. The mechanism by which TRPC1 suppressed TRPV6-mediated currents was through the sequestration of TRPV6 inside the cell and away from the plasma membrane (Schindl et al 2012). However, TRPC1 suppressed TRPV6 activity in Xenopus laevis oocytes by a mechanism different than cytosolic sequestration, as TRPV6 was detected in the plasma membrane of frog oocytes in the presence of TRPC1 (Courjaret et al 2013).…”

Section: Trpv6mentioning

confidence: 98%

“…TRPC1β lacking the N-terminal extension was shown to physically interact with TRPV6 in transfected cells (Schindl et al 2012). The interaction was mediated by the N-terminal ankyrin repeats of the two proteins and resulted in the reduction of TRPV6-mediated currents in transfected HEK293 cells.…”

Section: Trpv6mentioning

confidence: 99%

Trpc1

Nesin

Tsiokas

2014

Handbook of Experimental Pharmacology

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The TRPC1 ion channel was the first mammalian TRP channel to be cloned. In humans, it is encoded by the TRPC1 gene located in chromosome 3. The protein is predicted to consist of six transmembrane segments with the N- and C-termini located in the cytoplasm. The extracellular loop connecting transmembrane segments 5 and 6 participates in the formation of the ionic pore region. Inside the cell, TRPC1 is present in the endoplasmic reticulum, plasma membrane, intracellular vesicles, and primary cilium, an antenna-like sensory organelle functioning as a signaling platform. In human and rodent tissues, it shows an almost ubiquitous expression. TRPC1 interacts with a diverse group of proteins including ion channel subunits, receptors, and cytosolic proteins to mediate its effect on Ca(2+) signaling. It primarily functions as a cation nonselective channel within pathways controlling Ca(2+) entry in response to cell surface receptor activation. Through these pathways, it affects basic cell functions, such as proliferation and survival, differentiation, secretion, and cell migration, as well as cell type-specific functions such as chemotropic turning of neuronal growth cones and myoblast fusion. The biological role of TRPC1 has been studied in genetically engineered mice where the Trpc1 gene has been experimentally ablated. Although these mice live to adulthood, they show defects in several organs and tissues, such as the cardiovascular, central nervous, skeletal and muscular, and immune systems. Genetic and functional studies have implicated TRPC1 in diabetic nephropathy, Parkinson's disease, Huntington's disease, Duchenne muscular dystrophy, cancer, seizures, and Darier-White skin disease.

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Canonical Transient Receptor Potential (TRPC) 1 Acts as a Negative Regulator for Vanilloid TRPV6-mediated Ca2+ Influx

Cited by 46 publications

References 52 publications

TRPV6 calcium channel translocates to the plasma membrane via Orai1-mediated mechanism and controls cancer cell survival

TRPV6 calcium channel translocates to the plasma membrane via Orai1-mediated mechanism and controls cancer cell survival

Transient Receptor Potential Channels as Drug Targets: From the Science of Basic Research to the Art of Medicine

Trpc1

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