Endogenously Expressed Trp1 Is Involved in Store-mediated Ca2+ Entry by Conformational Coupling in Human Platelets

Rosado, Juan A.; Brownlow, Sharon; Sage, Stewart O.

doi:10.1074/jbc.m207320200

Cited by 138 publications

(134 citation statements)

References 37 publications

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“…6, C and D; p Ͻ 0.05; n ϭ 7). Electrotransjection of anti-STIM1 antibody inhibited SOCE and the coupling between hTRPC1 and IP 3 RII to a similar extent, which supports previous studies reporting that the coupling between hTRPC1 and IP 3 RII might underlie the activation of SOCE in human platelets (33). Electrotransjection of anti-STIM1 antibody did not significantly alter TG ϩ Iono-induced Ca 2ϩ release (the integral for 3 min of the rise in [Ca 2ϩ ] i after the addition of TG ϩ Iono was 7391 Ϯ 918 nM⅐s; Fig.…”

Section: Inhibition Of Store Depletion-evoked Interaction Between Stisupporting

confidence: 78%

“…After immunoprecipitation with antihTRPC1 antibody, Western blotting revealed the presence of STIM1 in samples from resting platelets. The specificity of the hTRPC1 antibody was tested with the anti-TRPC1 antibody T1E3, which has been shown to be a specific tool in the investigation of mammalian TRPC1 proteins (32,33). We found that store depletion increased the association between STIM1 and hTRPC1 by 50% (Fig.…”

Section: Presence and Localization Of Stim1 In Human Platelets-mentioning

confidence: 89%

“…Role of the Actin Cytoskeleton in the Association between STIM1 and hTRPC1-The de novo conformational coupling described in platelets to account for the activation of SOCE is based on the reversible interaction between elements in the ER and the PM that requires cytoskeletal reorganization (7,12,33,34,36). We have reported above that STIM1 both associates with the actin cytoskeleton and migrates to the cell surface upon store depletion, the later requiring actin remodeling.…”

Section: Presence and Localization Of Stim1 In Human Platelets-mentioning

confidence: 99%

“…Association between STIM1 and hTRPC1-Platelets have been shown to endogenously express hTRPC1 channel in the PM, as well as vascular smooth muscle cells (32), and a functional interaction between IP 3 RII in the Ca 2ϩ stores and hTRPC1 has been presented as the most likely mechanism to account for the activation of SOCE in these cells (12,(33)(34)(35). Since STIM1 have been proposed to communicate the Ca 2ϩ stores with Ca 2ϩ channels in the PM, the characteristics reported make platelets an ideal cellular model to investigate the interaction between proteins in the Ca 2ϩ stores and PM; therefore, we have tested for the association between STIM1 and hTRPC1 by looking for co-immunoprecipitation from platelet lysates.…”

Section: Presence and Localization Of Stim1 In Human Platelets-mentioning

confidence: 99%

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Interaction of STIM1 with Endogenously Expressed Human Canonical TRP1 upon Depletion of Intracellular Ca2+ Stores

López¹,

Salido

Pariente

et al. 2006

Journal of Biological Chemistry

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Section: Inhibition Of Store Depletion-evoked Interaction Between Stisupporting

confidence: 78%

Section: Presence and Localization Of Stim1 In Human Platelets-mentioning

confidence: 89%

Section: Presence and Localization Of Stim1 In Human Platelets-mentioning

confidence: 99%

Section: Presence and Localization Of Stim1 In Human Platelets-mentioning

confidence: 99%

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Interaction of STIM1 with Endogenously Expressed Human Canonical TRP1 upon Depletion of Intracellular Ca2+ Stores

López¹,

Salido

Pariente

et al. 2006

Journal of Biological Chemistry

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191

139

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“…9 and unpublished observations); (ii) lysophospholipids, such as lysophosphatidylcholine, shown for TRPC5 in ref. 13; (iii) conformational coupling by which the IP3-IP3 receptor complex activates TRPCs through direct protein-protein interaction (10)(11)(12); (iv) translocation of membrane vesicles by which TRPCs located in intracellular vesicles are shuttled to the plasma membrane (shown for TRPC5 in ref. 14); and (v) other as yet undefined mechanisms.…”

mentioning

confidence: 99%

Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/TRPC model for SOCE/Icrac channels

Liao

Erxleben

Abramowitz

et al. 2008

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

267

217

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Receptor-operated Ca 2؉ entry (ROCE) and store-operated Ca 2؉ entry (SOCE) into cells are functions performed by all higher eukaryotic cells, and their impairment is life-threatening. The main molecular components of this pathway appear to be known. However, the molecular make-up of channels mediating ROCE and SOCE is largely unknown. One hypothesis proposes SOCE channels to be formed solely by Orai proteins. Another proposes SOCE channels to be composed of both Orai and C-type transient receptor potential (TRPC) proteins. Both hypotheses propose that the channels are activated by STIM1, a sensor of the filling state of the Ca 2؉ stores that activates Ca 2؉ entry when stores are depleted. The role of Orai in SOCE has been proven. Here we show the TRPC-dependent reconstitution of Icrac, the electrophysiological correlate to SOCE, by expression of Orai1; we also show that R91W-Orai1 can inhibit SOCE and ROCE and that Orai1 and STIM1 expression leads to functional expression of Gd-resistant ROCE. Because channels that mediate ROCE are accepted to be formed with the participation of TRPCs, our data show functional interaction between ROCE and SOCE components. We propose that SOCE/Icrac channels are composed of heteromeric complexes that include TRPCs and Orai proteins.capacitative calcium entry ͉ signal transduction ͉ store depletion R eported independently by three laboratories at the beginning of 2006, Orai (also known as CRACM) proteins, especially Orai1, have emerged as the molecular candidates for the underlying structure of store-operated Ca 2ϩ entry (SOCE) channels responsible for the store-depletion activated Ca 2ϩ current, Icrac, without apparent role(s) for transient receptor potential ion channels (TRPCs) (reviewed in refs. 1-3). Before the discovery of Orai genes and their gene products, the only candidates presumed to underlie SOCE had been the members of the TRPC class of ion channels, of which there are seven. This proposition was based on primary research reports from many laboratories showing that expression of the cloned TRPCs enhances store-depletion activated Ca 2ϩ entry (cf. table 1.3 in ref. 4) and/or that injection of specific anti-TRPC antibodies or genetic ablation of TRPC genes reduces SOCE and/or Icrac. Moreover, Zagranichnaya et al. (5) showed partial reduction of SOCE in response to siRNAs that targeted TRPC1, TRPC3, or TRPC7, which, when combined, were partially additive. The idea promoted in the reviews listed above that channels responsible for SOCE and Icrac form without involvement of TRPC proteins is especially difficult to reconcile with the total loss of Icrac in vascular endothelial cells seen in TRPC4 knock-out mice (6) and the 80% loss of SOCE found in submaxillary acinar cells of TRPC1 knockout mice (7).Based on the foregoing data, and recognizing that Orai/ CRACMs are part of SOCE/Icrac channels, we proposed that SOCE/Icrac channels may be heteromeric complexes of TRPC and Orai proteins (8). If this were the case, we reasoned, expression of Orai1 in cells expressing excess ...

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Homer Proteins in Ca²⁺ Entry

et al. 2013

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The Homer family of proteins consists of three adaptor proteins, Homer1, Homer2 and Homer3, each with various isoforms. Homer1 family presents an EVH1 domain, a coiled coil domain and two leucine zipper domains. Homer proteins regulate a number of Ca21-handling proteins, including transient receptor potential channels and other Ca21-permeable channels, ionotropic and metabotropic glutamate receptors, shank scaffolding proteins or endoplasmic reticulum Ca21 release channels. This review article focuses on the association of Homer 1 proteins with Ca21-handling proteins and their role on intracellular Ca21-homeostasis. V C 2013 IUBMB Life, 65(6): [497][498][499][500][501][502][503][504] 2013

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Endogenously Expressed Trp1 Is Involved in Store-mediated Ca2+ Entry by Conformational Coupling in Human Platelets

Cited by 138 publications

References 37 publications

Interaction of STIM1 with Endogenously Expressed Human Canonical TRP1 upon Depletion of Intracellular Ca2+ Stores

Interaction of STIM1 with Endogenously Expressed Human Canonical TRP1 upon Depletion of Intracellular Ca2+ Stores

Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/TRPC model for SOCE/Icrac channels

Homer Proteins in Ca²⁺ Entry

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Endogenously Expressed Trp1 Is Involved in Store-mediated Ca2+ Entry by Conformational Coupling in Human Platelets

Cited by 138 publications

References 37 publications

Interaction of STIM1 with Endogenously Expressed Human Canonical TRP1 upon Depletion of Intracellular Ca2+ Stores

Interaction of STIM1 with Endogenously Expressed Human Canonical TRP1 upon Depletion of Intracellular Ca2+ Stores

Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/TRPC model for SOCE/Icrac channels

Homer Proteins in Ca2+ Entry

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Homer Proteins in Ca²⁺ Entry