Human inositol 1,4,5-trisphosphate type-1 receptor, Ins<i>P</i>3R1: structure, function, regulation of expression and chromosomal localization

Yamada, Nobuhiro; Makino, Yasutaka; Clark, Robert A.; Pearson, Doran W.; Mattéi, Marie Geneviève; Guénet, Jean-Louis; Ohama, Eisaku; Fujino, Ichiroh; Miyawaki, Atsushi; Furuichi, Teiichi; Mikoshiba, Katsuhiko

doi:10.1042/bj3020781

Cited by 117 publications

(59 citation statements)

References 65 publications

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“…Interestingly, as calreticulin transcripts decreased, those for the type I IP 3 receptor actually increased. Up-regulation of the IP 3 receptor under these circumstances, although well described previously (54,55), is curious, given the co-localization of the receptor with calreticulin in the ER Ca 2ϩ storage organelles and the shared functional participation of the two proteins in stimulus-mediated Ca 2ϩ release. The decrease in calreticulin mRNA during differentiation of myeloid cells could not be ascribed to increased catabolism of the transcripts.…”

Section: Fig 8 Immunoblot Analysis Of Selected Er and Cytosolic Promentioning

confidence: 84%

Regulation of Calreticulin Expression during Induction of Differentiation in Human Myeloid Cells

Clark¹,

Li²,

Pearson³

et al. 2002

Journal of Biological Chemistry

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Induction of differentiation of HL-60 human myeloid cells profoundly affected expression of calreticulin, a Ca2؉ -binding endoplasmic reticulum chaperone. Induction with Me 2 SO or retinoic acid reduced levels of calreticulin protein by ϳ60% within 4 days. Pulse-chase studies indicated that labeled calreticulin decayed at similar rates in differentiated and undifferentiated cells (t1 ⁄2 ϳ4.6 days), but the biosynthetic rate was <10% of control after 4 days. Differentiation also induced a rapid decline in calreticulin mRNA levels (90% reduction after 1 day) without a decrease in transcript stability (t1 ⁄2 ϳ5 h). Nuclear run-on analysis demonstrated rapid downregulation of gene transcription (21% of control at 2 h). Differentiation also greatly reduced the Ca 2؉ content of the cells (25% of control), although residual Ca 2؉ pools remained sensitive to thapsigargin, ionomycin, and inositol trisphosphate. Progressive decreases were also observed in levels of calnexin and ERp57, whereas BiP/ GRP78 and protein disulfide isomerase were only modestly affected. Ultrastructural studies showed a substantial reduction in endoplasmic reticulum content of the cells. Thus, terminal differentiation of myeloid cells was associated with decreased endoplasmic reticulum content, selective reductions in molecular chaperones, and diminished intracellular Ca 2؉ stores, perhaps reflecting an endoplasmic reticulum remodeling program as a prominent feature of granulocytic differentiation.Calreticulin is a major Ca 2ϩ -binding protein present in the lumen of the endoplasmic reticulum (ER) 1 of virtually all cell types (1-3). The cDNA sequence predicts an ϳ47-kDa acidic protein with a zonal structure featuring a globular N-terminal domain, a proline-rich P domain, and a highly acidic C domain terminating in a KDEL motif, the ER retention signal (3, 4).Biophysical studies show calreticulin to be a highly asymmetric molecule consistent with this predicted three domain structure. Calreticulin binds Ca 2ϩ with both high and low affinities and with high capacity. A single high affinity site (K d ϳ1 M) is located within the P domain of the molecule and multiple low affinity sites (K d ϳ2 mM, 20 -25 mol of Ca 2ϩ /mol of protein) are present in the highly acidic C domain (3,4). The N domain contains at least one site for binding Zn 2ϩ , which appears to involve 4 of the histidine residues in this region (5, 6). Binding of these ions affects the conformation and stability of the protein (7).Numerous and apparently unrelated functions have been ascribed to calreticulin since it was first identified, but its roles in the regulation of Ca 2ϩ homeostasis and as a molecular chaperone of nascent glycoproteins are the two functions that have been most extensively characterized. Calreticulin appears to regulate intracellular Ca 2ϩ homeostasis through more than one mechanism. The high Ca 2ϩ -binding capacity of calreticulin suggests that it acts as a Ca 2ϩ store or buffer within the ER, and there is evidence that in at least some cell types it is a main so...

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Section: Fig 8 Immunoblot Analysis Of Selected Er and Cytosolic Promentioning

confidence: 84%

Regulation of Calreticulin Expression during Induction of Differentiation in Human Myeloid Cells

Clark¹,

Li²,

Pearson³

et al. 2002

Journal of Biological Chemistry

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“…The volume was adjusted to 50 µl with the same PCR buffer and 2 mM MgCl # and 0.15 µM of the primers. The primer sequences used to amplify specific SERCA2b [19], SERCA3a [39], SERCA3b [40], SERCA3c [23] and InsP $ -R types I [41], II [42] or III [43] and predicted sizes of each amplification product are summarized in Table 1. PCR was initiated by adding 1.25 units of AmpliTaq DNA polymerase and touch-down PCR was performed for 10 cycles with an annealing temperature decrement from 65 to 56 mC for SERCA3a-3c.…”

Section: Rna Extraction and Rt-pcrmentioning

confidence: 99%

Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study

Lacabaratz-Porret

Launay

Corvazier

et al. 2000

Biochemical Journal

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The endoplasmic reticulum (ER) plays a key role in Ca# + signalling through Ca# + release via inositol 1,4,5-trisphosphate receptors (InsP $ -Rs) and Ca# + uptake by sarco\endoplasmic reticulum Ca# + -ATPases (SERCAs). Here, we investigated the organization of platelet ER and its biogenesis during megakaryocytopoiesis. First, erythro\megakaryoblastic MEG 01, UT7, M-O7e and CHRF 288-11 cell lines, platelets and thrombopoietininduced UT7-Mpl cells were selected for the study of SERCA2b and SERCA3 proteins by Western blotting using the antibodies IID8 and PL\IM430, respectively. As judged by platelet glycoprotein IIIa (GPIIIa) expression, an increase in SERCA3 proteins was observed while that of SERCA2b remained unchanged throughout maturation. Second, these studies were extended to the newly described alternatively spliced SERCA3a-c RNAs and InsP $ -Rs using the in itro model of PMA-induced differentiation of MEG 01 cells. Time-course and dose-response studies showed a maximal approx. 4-fold up-regulation of SERCA3 proteins using 10 −) M PMA for 3 days, which paralleled induction of GPIIIa expression. SERCA3 induction was found to occur at the level of mRNA. The modulation of the different SERCA3 species (i.e. 3a, 3b and 3c) was isoform-specific : while

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“…4, B and C) (12,6, and 0.6 g) (lane 3) or testis (7, 3.5, and 0.35 g) (lane 4) were used for the detection with antibodies M159, M151, and KM1083, respectively. Antibody M159 was used in the presence of 14 g/ml of T604 m2 , which contains the SI m2 segment, to avoid cross-reaction with IP 3 R2 SI m2 ϩ .…”

Section: Expression and Purification Of The N-terminal 604 And 605 Ammentioning

confidence: 99%

Molecular Cloning of Mouse Type 2 and Type 3 Inositol 1,4,5-Trisphosphate Receptors and Identification of a Novel Type 2 Receptor Splice Variant

Iwai

Tateishi

Hattori

et al. 2005

Journal of Biological Chemistry

102

111

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Inositol 1,4,5-trisphosphate (IP 3 ) 1 is a second messenger generated by the phosphatidylinositol signaling cascade response to hormones, neurotransmitters, and growth factors (1) and causes Ca 2ϩ release from intracellular stores by binding to the IP 3 receptor (IP 3 R), which is an IP 3 -gated intracellular Ca 2ϩ release channel. Ca 2ϩ release in the cytoplasm occurs in complex spatial and temporal patterns, such as Ca 2ϩ waves and Ca 2ϩ oscillations, and regulates many cellular responses, including fertilization, muscle contraction, secretion, cell growth, differentiation, apoptosis, and synaptic plasticity (1).The IP 3 R family consists of three isoforms (IP 3 R1, IP 3 R2, and IP 3 R3) (2), and the primary structure of all three IP 3 R types has been determined in rat (3-5) and human (6 -9). Only a single type of IP 3 R was identified in frog (10), fly (11), starfish (12), lobster (13), and nematode (14). Three isoforms have been found to exist in the mouse (15, 16), but the primary structure of mouse IP 3 R2 and IP 3 R3 has not yet been determined.IP 3 -gated Ca 2ϩ release channels are composed of four subunits (17). The expression levels of the three IP 3 R isoforms are different in each tissue, but most tissues contain multiple isoforms (18). Heterotetrameric channels were detected as well as homotetrameric channels (19), indicating that the structural diversity of the IP 3 -gated channels is greater than the number of genes. There is evidence of functional differences among the three types of IP 3 R in terms of their IP 3 sensitivity (20, 21) and the modulatory effects on them from cytoplasmic Ca 2ϩ (22), ATP (22), calmodulin (23), and cAMP-dependent protein kinase (24). Additional diversity of IP 3 -gated channels is produced by alternative splicing, and alternative splicing segments, designated SI, SII, and SIII, have been found in the mouse (25), rat (26), and human (9) IP 3 R1. These findings suggest that the channels composed of different isoforms possess distinctive functions, but little is known about the physiological significance and exact functional differences arising from the heterotetrameric assembly of IP 3 R.In many cells, the Ca 2ϩ increase triggered by IP 3 is propagated throughout the cytoplasm; however, the diffusion of free Ca 2ϩ is spatially restricted because many immobile or slowly diffusing Ca 2ϩ -binding proteins are present in the cytoplasm (27). Propagation of Ca 2ϩ is thought to be mediated by regenerative Ca 2ϩ release through IP 3 Rs, which are regulated by cytoplasmic Ca 2ϩ (28). Positive feedback regulation of IP 3 R by Ca 2ϩ enables the Ca 2ϩ released by one receptor to excite its

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Human inositol 1,4,5-trisphosphate type-1 receptor, InsP3R1: structure, function, regulation of expression and chromosomal localization

Cited by 117 publications

References 65 publications

Regulation of Calreticulin Expression during Induction of Differentiation in Human Myeloid Cells

Regulation of Calreticulin Expression during Induction of Differentiation in Human Myeloid Cells

Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study

Molecular Cloning of Mouse Type 2 and Type 3 Inositol 1,4,5-Trisphosphate Receptors and Identification of a Novel Type 2 Receptor Splice Variant

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