Microtubule-dependent redistribution of the type-1 inositol 1,4,5-trisphosphate receptor in A7r5 smooth muscle cells

Vermassen, Elke; Acker, K. Van; Annaert, Wim; Himpens, Bernard; Callewaert, Geert; Missiaen, Ludwig; Smedt, Humbert De; Parys, Jan B.

doi:10.1242/jcs.00354

Cited by 39 publications

(34 citation statements)

References 48 publications

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“…It remains to be determined whether this model of perinuclear Ca 2+ release is involved in regulating gene transcription and other nuclear activities in other cell types. However, there are numerous studies that have examined InsP 3 R distribution in various cell types and shown that these Ca 2+ channels are often most densely concentrated around the nucleus (Bootman et al, 2001;Shirakawa and Miyazaki, 1996;Thomas et al, 2000a;Vermassen et al, 2003). It therefore seems probable that modulation of nucleoplasmic Ca 2+ concentration by perinuclear Ca 2+ release is a generic signalling paradigm.…”

Section: Measuring Nuclear Ca 2+ Signals: Key Considerationsmentioning

confidence: 99%

An update on nuclear calcium signalling

Bootman

Fearnley

Smyrnias

et al. 2009

Journal of Cell Science

189

194

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Over the past 15 years or so, numerous studies have sought to characterise how nuclear calcium (Ca 2+ ) signals are generated and reversed, and to understand how events that occur in the nucleoplasm influence cellular Ca 2+ activity, and vice versa. In this Commentary, we describe mechanisms of nuclear Ca 2+ signalling and discuss what is known about the origin and physiological significance of nuclear Ca 2+ transients. In particular, we focus on the idea that the nucleus has an autonomous Ca 2+ signalling system that can generate its own Ca 2+ transients that modulate processes such as gene transcription. We also discuss the role of nuclear pores and the nuclear envelope in controlling ion flux into the nucleoplasm. Journal of Cell Science 2338(which would cause its nuclear export) and through a physical interaction that occludes a nuclear-export sequence (NES) in the NFAT protein.An example of a nuclear-localised transcription factor that is regulated by both nuclear and cytosolic Ca 2+ signals is cyclic AMP response element-binding protein (CREB). The signalling mechanisms that underlie CREB activation have been worked out particularly well in neurons, in which it has been established that depolarisation leads to the rapid phosphorylation of CREB on Ser133 by Ca 2+ -calmodulin-dependent kinase IV, which provides a necessary, but not sufficient, signal for CREB-mediated gene transcription (Dolmetsch et al., 2001). The triggering event is an increase in cytosolic Ca 2+ levels in the immediate vicinity of L-type Ca 2+ channels or N-methyl-D-aspartate receptors that are found in the synapse, at a site that is distal to the nucleus (Shaywitz and Greenberg, 1999). As CREB is only found in the nucleus, the phosphorylation of Ser133 is mediated by one of several Ca 2+ -sensitive signal transduction cascades that convey information from the remote synapses into the nucleus. In the nucleus, phosphorylated CREB binds additional proteins to form a transcriptionally active complex (Shaywitz and Greenberg, 1999). Although the synaptic Ca 2+ signal does not need to propagate to the nucleus to induce phosphorylation of Ser133 on CREB, an increase in the level of nuclear Ca 2+ is required for CREB-mediated gene transcription to occur. This is because additional Ca 2+ -dependent phosphorylation of CREB and its co-activators is required (Chawla et al., 1998;Kornhauser et al., 2002). Indeed, nuclear injection of an artificial Ca 2+ buffer prevents CREB-mediated gene transcription, but not transcription induced by the serum-response element, which is sensitive to cytosolic Ca 2+ buffering (Hardingham et al., 1997).Another well-known target of nuclear Ca 2+ signalling is the transcriptional regulator downstream regulatory element antagonist modulator (DREAM). It is well established that DREAM represses the expression of prodynorphin, an opiate-receptor precursor, and that mice that lack DREAM have a constitutive analgesic condition (Cheng et al., 2002). DREAM contains four Ca 2+ -binding EF hands (a widely expressed structural mo...

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Section: Measuring Nuclear Ca 2+ Signals: Key Considerationsmentioning

confidence: 99%

An update on nuclear calcium signalling

Bootman

Fearnley

Smyrnias

et al. 2009

Journal of Cell Science

189

194

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“…Ins(1,4,5)P 3 -evoked inotropy and arrhythmias use the membrane-permeant Ins(1,4,5)P 3 ester first introduced by Tsien and colleagues (Li et al, 1997). We (Chen et al, 2004;Kasri et al, 2004;Mackenzie et al, 2002;Peppiatt et al, 2003) and several other groups (Johenning et al, 2002;Tovey et al, 2003;Vermassen et al, 2003) have used the Ins(1,4,5)P 3 ester to specifically activate Ins(1,4,5)P 3 R-mediated Ca 2+ release. All reported effects of Ins(1,4,5)P 3 ester are consistent with a sole action of the compound on Ins(1,4,5)P 3 Rs.…”

Section: Characterisation Of Sctsmentioning

confidence: 99%

Inositol 1,4,5-trisphosphate supports the arrhythmogenic action of endothelin-1 on ventricular cardiac myocytes

Proven

Roderick

Conway

et al. 2006

Journal of Cell Science

110

111

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Although ventricular cardiomyocytes express inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] receptors, it is unclear how these Ca2+ channels contribute to the effects of Gq-coupled agonists. Endothelin-1 augmented the amplitude of pacing-evoked Ca2+ signals (positive inotropy), and caused an increasing frequency of spontaneous diastolic Ca2+-release transients. Both effects of endothelin-1 were blocked by an antagonist of phospholipase C, suggesting that Ins(1,4,5)P3 and/or diacylglycerol production was necessary. The endothelin-1-mediated spontaneous Ca2+ transients were abolished by application of 2-aminoethoxydiphenyl borate (2-APB), an antagonist of Ins(1,4,5)P3 receptors. Incubation of electrically-paced ventricular myocytes with a membrane-permeant Ins(1,4,5)P3 ester provoked the occurrence of spontaneous diastolic Ca2+ transients with the same characteristics and sensitivity to 2-APB as the events stimulated by endothelin-1. In addition to evoking spontaneous Ca2+ transients, stimulation of ventricular myocytes with the Ins(1,4,5)P3 ester caused a positive inotropic effect. The effects of endothelin-1 were compared with two other stimuli, isoproterenol and digoxin, which are known to induce inotropy and spontaneous Ca2+ transients by overloading intracellular Ca2+ stores. The events evoked by isoproterenol and digoxin were dissimilar from those triggered by endothelin-1 in several ways. We propose that Ins(1,4,5)P3 receptors support the development of both inotropy and spontaneous pro-arrhythmic Ca2+ signals in ventricular myocytes stimulated with a Gq-coupled agonist.

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“…Rather recently, evidence has been accumulating that the subcellular localization of IP 3 R is tightly controlled and changes according to circumstances (2)(3)(4). In addition, IP 3 R is known to form large clusters on the ER (5).…”

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confidence: 99%

Cluster Formation of Inositol 1,4,5-Trisphosphate Receptor Requires Its Transition to Open State

Tateishi

Hattori

Nakayama

et al. 2005

Journal of Biological Chemistry

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3 -induced conformational change to the open state. We also found that GFP-IP 3 R1 clusters colocalized with ERp44, a luminal protein of endoplasmic reticulum that inhibits its channel activity. This is the first example of ligandinduced clustering of a ligand-gated channel protein.Many extracellular stimuli are received by trimeric G protein-or tyrosine kinase-coupled receptors and relayed to signaling molecules including phospholipase C (PLC), 1 which leads to production of a second messenger, inositol 1,4,5-trisphosphate (IP 3 ) (1). IP 3 in turn activates an internal membrane receptor/Ca 2ϩ channel, the IP 3 receptor (IP 3 R), and induces Ca 2ϩ release from internal Ca 2ϩ stores (mostly endoplasmic reticulum (ER)). This IP 3 -Ca 2ϩ pathway is particularly important because it is located at the intersection of many signaling pathways and is therefore thought to play a central role in cellular signaling.Rather recently, evidence has been accumulating that the subcellular localization of IP 3 R is tightly controlled and changes according to circumstances (2-4). In addition, IP 3 R is known to form large clusters on the ER (5). Very importantly, theoretical modeling (6 -8) predicted that IP 3 R clustering affects both elementary events (e.g. Ca 2ϩ blips and puffs) and the formation of complex cytosolic Ca 2ϩ concentration ([Ca 2ϩ ] C ) patterns (e.g. Ca 2ϩ oscillations and waves). Particularly Shuai and Jung (6) predicted that if IP 3 concentration is relatively low (i.e. physiological situation), there is an optimal extent of clustering of IP 3 receptor for effective elevation of cytosolic calcium concentration. When the clusters of IP 3 receptor would become very large, the whole calcium signals elicited by low IP 3 concentrations would be significantly reduced. Experimental verification of this hypothesis has not been performed mainly because the molecular mechanism of IP 3 R clustering remains totally unknown, and thus it is impossible to inhibit or artificially modulate it. Wilson et al. (5) suggested that IP 3 R clustering was triggered by increased [Ca 2ϩ ] C since not only Ca 2ϩ -mobilizing agonists but a Ca 2ϩ ionophore (ionomycin) and an inhibitor of sarco/ endoplasmic Ca 2ϩ -ATPase (thapsigargin) induced it. They also showed that it is independent of ER vesiculation (9). Later it was shown that two small GTP-binding proteins, Cdc42 and Rac, are involved in agonist-induced IP 3 R clustering but that was because they augmented Ca 2ϩ signals as a whole and not because they influenced intracellular trafficking (10). In short, the detailed molecular mechanism of IP 3 R clustering remains largely unknown, and it is important to know it to understand precise roles of IP 3 R clustering. In this study we simultaneously imaged the dynamics of enhanced green fluorescent protein (GFP)-tagged IP 3 R type 1 (GFP-IP 3 R1) and [Ca 2ϩ ] C by using fluorescent Ca 2ϩ indicators. Based on the results of the mutational and pharmacological analyses, we concluded that IP 3 R clustering is initiated by a conformational c...

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Microtubule-dependent redistribution of the type-1 inositol 1,4,5-trisphosphate receptor in A7r5 smooth muscle cells

Cited by 39 publications

References 48 publications

An update on nuclear calcium signalling

An update on nuclear calcium signalling

Inositol 1,4,5-trisphosphate supports the arrhythmogenic action of endothelin-1 on ventricular cardiac myocytes

Cluster Formation of Inositol 1,4,5-Trisphosphate Receptor Requires Its Transition to Open State

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