The Xenopus IP3 receptor: Structure, function, and localization in oocytes and eggs

Kume, Shoen; Muto, Akira; Aruga, Jun; Nakagawa, Toshiyuki; Michikawa, Takayuki; Furuichi, Teiichi; Nakade, Shinji; Okano, Hideyuki; Mikoshiba, Katsuhiko

doi:10.1016/0092-8674(93)90142-d

Cited by 222 publications

(155 citation statements)

References 92 publications

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“…The bovine motif is homologous to what has been described as the center of nine variant nuclear localization sequences all of which contain the tetrameric consensus (R/K)x(R/K) [21,22]. This motif appears in this configuration or in slight variations in a number of proteins that are known to be translocated into the nucleus [23][24][25][26]. Moreover, and this is of particular interest, this NLS motif is also found in Tyk2 and JAK-1, two components of the Type 1 IFN signal transduction pathway [27,28].…”

Section: Discussionmentioning

confidence: 93%

Nuclear and cytoplasmic localization of interferon-τ in in vitro-produced bovine blastocysts

et al. 2006

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-Experiments were conducted to detect interferon-τ in bovine in vitro-derived blastocysts by transmission electron (TEM) and confocal microscopy. TEM showed the presence of IFN-τ in the cytoplasm and the nuclei of expanded blastocysts. Confocal microscopy similarly confirmed the presence of IFN-τ in the trophectoderm of blastocysts. The distribution of IFN-τ appeared variable with some cells showing strong labeling while others appeared to be devoid of the protein.interferon-τ / embryo / blastocyst / gene expression / IVF

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Section: Discussionmentioning

confidence: 93%

Nuclear and cytoplasmic localization of interferon-τ in in vitro-produced bovine blastocysts

et al. 2006

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“…The effect could be traced back to: (a) the increase in the amount of Ca 2ϩ trapped in the ER as shown in mouse oocytes (36); (b) the increase in the expression and/or redistribution of the InsP 3 receptors during the maturation process as previously described in Xenopus and mouse oocytes (36,37); and (c) changes in the InsP 3 receptors that increase their response to InsP 3 . Western blot analysis and immunohistochemistry have recently shown that the expression and the distribution of the InsP 3 receptors in A. pectinifera starfish oocytes did not change during the meiotic process (18).…”

Section: Modulation Of the Actin Cytoskeleton By Mpf Is Responsible Fmentioning

confidence: 84%

The M-phase-promoting Factor Modulates the Sensitivity of the Ca2+ Stores to Inositol 1,4,5-Trisphosphate via the Actin Cytoskeleton

Lim

Ercolano

Kyozuka³

et al. 2003

Journal of Biological Chemistry

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The resumption of the meiotic cycle (maturation) induced by 1-methyladenine in prophase-arrested starfish oocytes is indicated by the breakdown of the germinal vesicle and is characterized by the increased sensitivity of the Ca 2؉ stores to inositol 1,4,5-trisphosphate (InsP 3 ) to InsP 3 starting at the animal hemisphere (where the germinal vesicle was originally located) and propagating along the animal/vegetal axis of the oocyte. This initiates Ca 2؉ signals around the germinal vesicle before nuclear envelope breakdown. Previous studies have suggested that the final activation of the maturation-promoting factor (MPF), a cyclin-dependent kinase, which is the major element controlling the entry of eukaryotic cells into the M phase, occurs in the nucleus. MPF is then exported to the cytoplasm where its activity is autocatalytically amplified following a similar animal/vegetal spatial pattern. We have investigated whether activated MPF was involved in the increased sensitivity of the Ca 2؉ response to InsP 3 . We have found that the development of increased sensitivity of the Ca 2؉ stores to InsP 3 receptors together with the Ca 2؉ signals in the perinuclear region was blocked in oocytes treated with the specific MPF inhibitor roscovitine. That the nuclear MPF activation is indeed required for changes of the InsP 3 receptors sensitivity was shown by enucleating or by dissecting oocytes into vegetal and animal hemispheres prior to the addition of 1-MA. MPF activity 50 min after 1-methyladenine addition was much lower in the enucleated oocytes and in the vegetal hemisphere, which did not contain the germinal vesicle, as compared with the animal hemisphere, which did contain it. The Ca 2؉ increase induced by InsP 3 under these experimental conditions correlated with the changes in actin cytoskeleton induced by MPF.

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“…1A). We also performed immunoblot analysis of type 1 IP 3 receptors, the only type of calcium release channel expressed in Xenopus oocytes; this cell type does not express ryanodine receptors (Kume et al, 1993). Our analysis revealed that IP 3 receptor levels did not differ significantly among the experimental conditions (Fig.…”

Section: Expression Of Presenilin and Ip 3 Receptorsmentioning

confidence: 99%

Subcellular Mechanisms of Presenilin-Mediated Enhancement of Calcium Signaling

Leissring

LaFerla

Callamaras

et al. 2001

Neurobiology of Disease

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Mutations in presenilin-1 (PS1), the leading cause of early-onset, autosomal-dominant familial Alzheimer's disease (FAD), enhance calcium signaling mediated by inositol 1,4,5-trisphosphate (IP 3 ). To elucidate the subcellular mechanisms underlying this enhancement, we used high resolution linescanning confocal microscopy to image elementary calcium release events ("puffs") in Xenopus oocytes expressing wild-type or mutant PS1. Here we report that mutant PS1-rendered puffs more sensitive to IP 3 and increased both the magnitude and the rate of calcium release during each event. These effects were not attributable to quantitative changes in the levels of IP 3 receptors or their distribution on the ER, but were instead associated with an abnormal elevation of ER calcium stores. Together, our results suggest that the effects of mutant PS1 on calcium signaling are manifested predominantly at the level of the regulation of calcium stores rather than via perturbations in the numbers or activity of IP 3 -activated calcium release channels.

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The Xenopus IP3 receptor: Structure, function, and localization in oocytes and eggs

Cited by 222 publications

References 92 publications

Nuclear and cytoplasmic localization of interferon-τ in in vitro-produced bovine blastocysts

Nuclear and cytoplasmic localization of interferon-τ in in vitro-produced bovine blastocysts

The M-phase-promoting Factor Modulates the Sensitivity of the Ca2+ Stores to Inositol 1,4,5-Trisphosphate via the Actin Cytoskeleton

Subcellular Mechanisms of Presenilin-Mediated Enhancement of Calcium Signaling

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