Rapid vesicular translocation and insertion of TRP channels

Bezzerides, Vassilios J.; Ramsey, I. Scott; Kotecha, Suhas A.; Greka, Anna; Clapham, David E.

doi:10.1038/ncb1150

Cited by 493 publications

(502 citation statements)

References 51 publications

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“…Stimulation of the M3 receptor causes the translocation of TRPC6 to the plasma membrane [51], and stimulation EGF receptor caused the translocation of TRPC4 [52] and TRPC5 [53] to the plasma membrane. The PI3-kinase pathway and its downstream effector Rac1 are implicated in the EGFstimulated translocation of TRPC5 [53], which may be a general mechanism mediating Tyrosine kinase receptor mediated translocation of TRPC channels.…”

Section: Homer1 and Translocation Of Trpc Channelsmentioning

confidence: 99%

Homer proteins in Ca2+ signaling by excitable and non-excitable cells

et al. 2007

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Homers are scaffolding proteins that bind Ca 2+ signaling proteins in cellular microdomains. The Homers participate in targeting and localization of Ca 2+ signaling proteins in signaling complexes. However, recent work showed that the Homers are not passive scaffolding proteins, but rather they regulate the activity of several proteins within the Ca 2+ signaling complex in an isoform specific manner. Homer2 increases the GAP activity of RGS proteins and PLCβ that accelerate the GTPase activity of Gα subunits. Homer1 gates the activity of TRPC channels, controls the rates of their translocation and retrieval from the plasma membrane and mediates the conformational coupling between TRPC channels and IP 3 Rs. Homer1 stimulates the activity of the cardiac and neuronal Ltype Ca 2+ channels Ca v 1.2 and Ca v 1.3. Homer1 also mediates the communication between the cardiac and smooth muscle ryanodine receptor RyR2 and Ca v 1.2 to regulate E-C coupling. In many cases the Homers function as a buffer to reduce the intensity of Ca 2+ signaling and create a negative bias that can be reversed by the immediate early gene form of Homer 1. Hence, the Homers should be viewed as the buffers of Ca 2+ signaling that ensure a high spatial and temporal fidelity of the Ca 2+ signaling and activation of downstream effects.

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Section: Homer1 and Translocation Of Trpc Channelsmentioning

confidence: 99%

Homer proteins in Ca2+ signaling by excitable and non-excitable cells

et al. 2007

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“…The mechanism of PKD2 activation by EGF appears to be different from the mechanism by which EGF activated another TRP channel, TRPC5. In the case of TRPC5, EGF acted through Rac1 to induce the activation of PIP(5)Kα and production of PIP 2 , which in turn promoted the vesicular translocation of TRPC5 from intracellular compartments to the plasma membrane [74]. Ma et al [36] proposed that both mechanisms may be functional in PKD2.…”

Section: Modes Of Pkd2 Activationmentioning

confidence: 99%

Cell biology of polycystin-2

Tsiokas¹,

Kim²,

Ong³

2007

Cellular Signalling

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Naturally occurring mutations in two separate, but interacting loci, pkd1 and pkd2 are responsible for almost all cases of autosomal dominant polycystic kidney disease (ADPKD). ADPKD is one of the most common genetic diseases resulting primarily in the formation of large kidney, liver, and pancreatic cysts. Homozygous deletion of either pkd1 or pkd2 results in embryonic lethality in mice due to kidney and heart defects illustrating their indispensable roles in mammalian development. However, the mechanism by which mutations in these genes cause ADPKD and other developmental defects are unknown. Research in the past several years has revealed that PKD2 has multiple functions depending on its subcellular localization. It forms a receptor-operated, non-selective cation channel in the plasma membrane, a novel intracellular Ca 2+ release channel in the endoplasmic reticulum (ER), and a mechanosensitive channel in the primary cilium. This review focuses on the functional compartmentalization of PKD2, its modes of activation, and PKD2-mediated signal transduction.

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“…To prevent saturation of the light response upon an increase in ambient light, the Ca 2+ flow via the Ca 2+ -selective TRP channel attenuates the nonselective cation channel, TRPL (Reuss et al, 1997), and also induces its translocation out of the signaling membranes (Bähner et al, 2002). This novel mechanism to fine-tune visual responses is also used by other cellular signaling mechanisms such as fine tuning of growth cone path finding due to the action of a growth factor on TRPC5 activation (Bezzerides et al, 2004).…”

Section: Light-regulated Translocation Of the Trpl Channelmentioning

confidence: 99%

“…Translocation of TRP channels of both Drosophila and mammalian cells (Bähner et al, 2002;Bezzerides et al, 2004;Boels et al, 2001;Kanzaki et al, 1999) emerges as a novel and important regulatory mechanism with wide implications to a variety of signaling mechanisms.…”

Section: Light-regulated Translocation Of the Trpl Channelmentioning

confidence: 99%

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

Frechter

Minke

2006

Journal of Physiology-Paris

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Illumination of Drosophila photoreceptor cells induces multi-facet responses, which include generation of the photoreceptor potential, screening pigment migration and translocation of signaling proteins which is the focus of recent extensive research. Translocation of three signaling molecules is covered in this review: (1) Light-dependent translocation of arrestin from the cytosol to the signaling membrane, the rhabdomere, determines the lifetime of activated rhodopsin. Arrestin translocates in PIP 3 and NINAC myosin III dependent manner, and specific mutations which disrupt the interaction between arrestin and PIP 3 or NINAC also impair the light-dependant translocation of arrestin and the termination of the response to light. (2) Activation of Drosophila visual G protein, DGq, causes a massive and reversible, translocation of the α subunit from the signaling membrane to the cytosol, accompanied by activity-dependent architectural changes. Analysis of the translocation and the recovery kinetics of DGq α in wild-type flies and specific visual mutants indicated that DGq α is necessary but not sufficient for the architectural changes. (3) The TRP-like (TRPL) but not TRP channels translocate in a light-dependent manner between the rhabdomere and the cell body. As a physiological consequence of this light-dependent modulation of the TRP/TRPL ratio, the photoreceptors of dark-adapted flies operate at a wider dynamic range, which allows the photoreceptors enriched with TRPL to function better in darkness and dim background illumination. Altogether, signal-dependent movement of signaling proteins plays a major role in the maintenance and function of photoreceptor cells.

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Rapid vesicular translocation and insertion of TRP channels

Cited by 493 publications

References 51 publications

Homer proteins in Ca2+ signaling by excitable and non-excitable cells

Homer proteins in Ca2+ signaling by excitable and non-excitable cells

Cell biology of polycystin-2

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

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