Identification and subcellular distribution of endogenous Ins(1,4,5)P3 3-kinase B in mouse tissues

Hascakova-Bartova, Romana; Pouillon, Valérie; Dewaste, Valérie; Moreau, Colette; Jacques, Caroline; Banting, George; Schurmans, Stéphane; Erneux, Christophé

doi:10.1016/j.bbrc.2004.08.152

Cited by 11 publications

(5 citation statements)

References 23 publications

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“…Nevertheless, recent experimental evidence supports the general idea that ITPKB is regulated by proteolysis, with the functional consequence being that proteolysis changes the enzyme's subcellular localization [74,75]. When full-length ITPKB is expressed in cells, it exhibits a heterogeneous localization and occurs with different molecular weights [50,[74][75][76]. Depending on the cell, ITPKB is associated with the actin cytoskeleton, on intracellular membranes, or in the cytosol.…”

Section: Regulation By Proteolysis and Intracellular Targetingmentioning

confidence: 96%

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Inositol trisphosphate 3-kinases: focus on immune and neuronal signaling

Schell

2010

Cell. Mol. Life Sci.

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The localized control of second messenger levels sculpts dynamic and persistent changes in cell physiology and structure. Inositol trisphosphate [Ins(1,4,5)P(3)] 3-kinases (ITPKs) phosphorylate the intracellular second messenger Ins(1,4,5)P(3). These enzymes terminate the signal to release Ca(2+) from the endoplasmic reticulum and produce the messenger inositol tetrakisphosphate [Ins(1,3,4,5)P(4)]. Independent of their enzymatic activity, ITPKs regulate the microstructure of the actin cytoskeleton. The immune phenotypes of ITPK knockout mice raise new questions about how ITPKs control inositol phosphate lifetimes within spatial and temporal domains during lymphocyte maturation. The intense concentration of ITPK on actin inside the dendritic spines of pyramidal neurons suggests a role in signal integration and structural plasticity in the dendrite, and mice lacking neuronal ITPK exhibit memory deficits. Thus, the molecular and anatomical features of ITPKs allow them to regulate the spatiotemporal properties of intracellular signals, leading to the formation of persistent molecular memories.

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Section: Regulation By Proteolysis and Intracellular Targetingmentioning

confidence: 96%

“…response [45,76] (see later section). Isoform B (ITPKB) is widely expressed [50], with notably high levels in immune tissues. Mice lacking ITPKB exhibit major deficits in lymphocyte maturation [51,52], neutrophil activation [53], and myelopoiesis [54].…”

Section: )P 3 Onlymentioning

confidence: 99%

Inositol trisphosphate 3-kinases: focus on immune and neuronal signaling

Schell

2010

Cell. Mol. Life Sci.

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“…Recently, the localization of IP3KB has been studied in more detail [13], including the identification of a binding domain for Factin [14] and the determination of putative proteolytic cleavage sites [15]. With regard to the subcellular location, early expression studies using an N-terminally truncated enzyme showed IP3KB to be associated with the ER (endoplasmic reticulum) membrane [16], whereas more recent studies have suggested an association with F-actin on the plasma membrane [14] or a mixed localization [15,17].…”

Section: Introductionmentioning

confidence: 99%

Regulation of the localization and activity of inositol 1,4,5-trisphosphate 3-kinase B in intact cells by proteolysis

Lloyd-Burton

Irvine

et al. 2005

Biochemical Journal

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IP3K (inositol 1,4,5-trisphosphate 3-kinase) catalyses the Ca2+-regulated phosphorylation of the second messenger Ins(1,4,5)P3, thereby inactivating the signal to release Ca2+ and generating Ins(1,3,4,5)P4. Here we have investigated the localization and activity of IP3KB and its modulation by proteolysis. We found that the N- and C-termini (either side of residue 262) of IP3KB localized predominantly to the actin cytoskeleton and ER (endoplasmic reticulum) respectively, both in COS-7 cells and in primary astrocytes. The functional relevance of this was demonstrated by showing that full-length (actin-localized) IP3KB abolished the histamine-induced Ca2+ response in HeLa cells more effectively than truncated constructs localized to the ER or cytosol. The superior efficacy of full-length IP3KB was also attenuated by disruption of the actin cytoskeleton. By transfecting COS-7 cells with double-tagged IP3KB, we show that the translocation from actin to ER may be a physiologically regulated process caused by Ca2+-modulated constitutive proteolysis in intact cells.

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“…Human lung carcinoma cell line H1299, human melanoma cell line Mevo, human mammary adenocarcinoma cell line T47D, and normal rat kidney tubular epithelial cell line NRK52E clearly showed expression of full-length IP3K-C ( Figure 1B). This potential product of proteolytic degradation was also observed in IP3K-C transfected COS-7 cells by Hascakova- Bartova et al (2004). The antibody also recognises an additional band corresponding to a protein of approximately 60 kDa.…”

Section: Endogenous Expression Of Ip3k-c In Mammalian Cell Linesmentioning

confidence: 52%

Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains

Nalaskowski

Windhorst²,

Stockebrand³

et al. 2006

Biological Chemistry

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The three isoforms of human Ins(1,4,5)P3 3-kinase (IP3K) show remarkable differences in their intracellular targeting. Whereas predominant targeting to the cytoskeleton and endoplasmic reticulum has been shown for IP3K-A and IP3K-B, rat IP3K-C shuttles actively between the nucleus and cytoplasm. In the present study we examined the expression and intracellular localisation of endogenous IP3K-C in different mammalian cell lines using an isoform-specific antibody. In addition, human IP3K-C, showing remarkable differences to its rat homologue in the N-terminal targeting domain, was tagged with EGFP and used to examine active transport mechanisms into and out of the nucleus. We found both a nuclear import activity residing in its N-terminal domain and a nuclear export activity sensitive to treatment with leptomycin B. Different from the rat isoform, an exportin 1-dependent nuclear export site of the human enzyme resides outside the N-terminal targeting domain in the catalytic enzyme domain. A phylogenetic survey of vertebrate IP3K sequences indicates that in each of the three isoforms a nuclear export signal has evolved in the catalytic domain either de novo (IP3K-A) or as a substitute for an earlier evolved corresponding N-terminal signal (IP3K-B and IP3K-C). In higher vertebrates, and in particular in primates, re-export of nuclear IP3K activity may be guaranteed by the mechanism discovered.

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Identification and subcellular distribution of endogenous Ins(1,4,5)P3 3-kinase B in mouse tissues

Cited by 11 publications

References 23 publications

Inositol trisphosphate 3-kinases: focus on immune and neuronal signaling

Inositol trisphosphate 3-kinases: focus on immune and neuronal signaling

Regulation of the localization and activity of inositol 1,4,5-trisphosphate 3-kinase B in intact cells by proteolysis

Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains

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