STIM1 converts TRPC1 from a receptor-operated to a store-operated channel: Moving TRPC1 in and out of lipid rafts

Sampieri, Alicia; Zepeda, Angélica; Saldaña, Carlos; Salgado-Aguayo, Alfonso; Vaca, Luis

doi:10.1016/j.ceca.2008.03.001

Cited by 120 publications

(98 citation statements)

References 35 publications

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“…Further, we demonstrated that peripheral STIM1 puncta are anchored in LRD which facilitates TRPC1-STIM1 association required for activation of TRPC1-SOCE (6). This has now been suggested in several other studies (10,18,23). The role of LRD in the regulation of TRPC1-SOC suggested by these recent findings are consistent with previous reports which showed that plasma membrane localization of TRPC1 depends on its association with the cholesterol-binding protein caveolin-1 (Cav1), which promotes retention of TRPC1 within the LRD (6,18,[22][23][24][25].…”

supporting

confidence: 81%

“…This has now been suggested in several other studies (10,18,23). The role of LRD in the regulation of TRPC1-SOC suggested by these recent findings are consistent with previous reports which showed that plasma membrane localization of TRPC1 depends on its association with the cholesterol-binding protein caveolin-1 (Cav1), which promotes retention of TRPC1 within the LRD (6,18,(22)(23)(24)(25). Together, these findings suggest a critical role for Cav1 and LRD in the association of TRPC1 with STIM1 within ER-PM junctional regions that is required for SOCE (10,(26)(27)(28).…”

mentioning

confidence: 66%

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Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1

Pani

Ong

Brazer

et al. 2009

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

120

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Store-operated Ca 2؉ entry (SOCE) is activated by redistribution of STIM1 into puncta in discrete ER-plasma membrane junctional regions where it interacts with and activates store-operated channels (SOCs). The factors involved in precise targeting of the channels and their retention at these specific microdomains are not yet defined. Here we report that caveolin-1 (Cav1) is a critical plasma membrane scaffold that retains TRPC1 within the regions where STIM1 puncta are localized following store depletion. This enables the interaction of TRPC1 with STIM1 that is required for the activation of TRPC1-SOCE. Silencing Cav1 in human submandibular gland (HSG) cells decreased plasma membrane retention of TRPC1, TRPC1-STIM1 clustering, and consequently reduced TRPC1-SOCE, without altering STIM1 puncta. Importantly, activation of TRPC1-SOCE was associated with an increase in TRPC1-STIM1 and a decrease in TRPC1-Cav1 clustering. Consistent with this, overexpression of Cav1 decreased TRPC1-STIM1 clustering and SOCE, both of which were recovered when STIM1 was expressed at higher levels relative to Cav1. Silencing STIM1 or expression of ⌬ERM-STIM1 or STIM1( 684 EE 685 ) mutant prevented dissociation of TRPC1-Cav1 and activation of TRPC1-SOCE. However expression of TRPC1-( 639 KK 640 ) with STIM1( 684 EE 685 ) restored function and the dissociation of TRPC1 from Cav1 in response to store depletion. Further, conditions that promoted TRPC1-STIM1 clustering and TRPC1-SOCE elicited corresponding changes in SOCE-dependent NFkB activation and cell proliferation. Together these data demonstrate that Cav1 is a critical plasma membrane scaffold for inactive TRPC1. We suggest that activation of TRPC1-SOC by STIM1 mediates release of the channel from Cav1. S tore-operated calcium entry (SOCE) is activated by depletion of endoplasmic reticulum (ER) Ca 2ϩ stores and regulates a variety of critical cellular functions (1). Ca 2ϩ depletion in the ER lumen is detected by the Ca 2ϩ -binding protein STIM1, which oligomerizes into puncta and relocates to discrete ERplasma membrane (ER-PM) junctional regions (2, 3) where it associates with and activates store-operated channels including Orai1 and TRPC1, which are components of CRAC and SOC channels, respectively (4-13). Therefore, the location of these channels in the plasma membrane is likely to be critical for their interaction with peripheral STIM1 and activation. However, mechanisms involved in the precise targeting and retention of the channels at the domains where STIM1 puncta are located are not well-understood.Distinct regions of STIM1 determine aggregation and targeting of the protein to ER-PM junctional domains as well as its clustering with and gating of Orai1 and TRPC1 at these sites. The SAM and coiled-coiled domains are involved in STIM1 aggregation while the polybasic C-terminal region of STIM1 is suggested to target STIM1 to ER-PM junctional regions, which is the likely site for SOCE in native cells (3,(9)(10)(11)14). Thus, it can be predicted that SOCs are either localized in this...

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supporting

confidence: 81%

mentioning

confidence: 66%

Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1

Pani

Ong

Brazer

et al. 2009

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

120

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“…Conversely, TRPC1 silencing nearly abolishes outward I SOC , but it also reduces significantly the extent of the inward component. Consistently, it has been shown that STIM1 may drive interactions between ORAI1 and TRPC1 (39,50).…”

Section: Discussionsupporting

confidence: 48%

A Reciprocal Shift in Transient Receptor Potential Channel 1 (TRPC1) and Stromal Interaction Molecule 2 (STIM2) Contributes to Ca2+ Remodeling and Cancer Hallmarks in Colorectal Carcinoma Cells

Sobradillo

Hernández-Morales

Ubierna

et al. 2014

Journal of Biological Chemistry

122

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“…In this regard, the association of STIM1 with TRPC1 favors the insertion of TRPC1 into lipid rafts, where it acts as a SOC channel, in contrast with the STIM1-independent activity of TRPC1 as a receptor-operated calcium channel that shows a regular distribution in the PM (Alicia et al 2008, Pani et al 2008. Whether this particular localization of STIM1 in oocytes under ER depletion stimuli is due to the segregation of STIM1 to PM domains enriched in lipid rafts is beyond the scope of this work, although this plausible hypothesis opens up a new window of studies on Ca 2C signaling at fertilization.…”

Section: M3fbs In Hbss (Green Line) (Panel B) Oocytes In Camentioning

confidence: 99%

Relocalization of STIM1 in mouse oocytes at fertilization: early involvement of store-operated calcium entry

Gómez-Fernández

Pozo‐Guisado²,

Gañán-Parra³

et al. 2009

Reproduction

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Calcium waves represent one of the most important intracellular signaling events in oocytes at fertilization required for the exit from metaphase arrest and the resumption of the cell cycle. The molecular mechanism ruling this signaling has been described in terms of the contribution of intracellular calcium stores to calcium spikes. In this work, we considered the possible contribution of store-operated calcium entry (SOCE) to this signaling, by studying the localization of the protein STIM1 in oocytes. STIM1 has been suggested to play a key role in the recruitment and activation of plasma membrane calcium channels, and we show here that mature mouse oocytes express this protein distributed in discrete clusters throughout their periphery in resting cells, colocalizing with the endoplasmic reticulum marker calreticulin. However, immunolocalization of the endogenous STIM1 showed considerable redistribution over larger areas or patches covering the entire periphery of the oocyte during Ca 2C store depletion induced with thapsigargin or ionomycin. Furthermore, pharmacological activation of endogenous phospholipase C induced a similar pattern of redistribution of STIM1 in the oocyte. Finally, fertilization of mouse oocytes revealed a significant and rapid relocalization of STIM1, similar to that found after pharmacological Ca 2C store depletion. This particular relocalization supports a role for STIM1 and SOCE in the calcium signaling during early stages of fertilization.

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STIM1 converts TRPC1 from a receptor-operated to a store-operated channel: Moving TRPC1 in and out of lipid rafts

Cited by 120 publications

References 35 publications

Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1

Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1

A Reciprocal Shift in Transient Receptor Potential Channel 1 (TRPC1) and Stromal Interaction Molecule 2 (STIM2) Contributes to Ca2+ Remodeling and Cancer Hallmarks in Colorectal Carcinoma Cells

Relocalization of STIM1 in mouse oocytes at fertilization: early involvement of store-operated calcium entry

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