Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei.

Matter, Nathalie; Ritz, Marie‐Françoise; Freyermuth, Solange; Rogue, P; Malviya, Anant N.

doi:10.1016/s0021-9258(18)54213-7

Cited by 127 publications

(19 citation statements)

References 34 publications

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“…Consistent with this, we and others have shown that PKC inhibition enhances hormoneinduced Ca 2+ signaling, whereas acute PKC activation with phorbol ester decreases Ca 2+ oscillation frequency (Bartlett et al, 2015;Sanchez-Bueno et al, 1990). PKC phosphorylation may also modify the activity of IP 3 Rs (Matter et al, 1993;Arguin et al, 2007), and thus has the potential to affect the onset or duration of class 1 oscillations. Indeed, we have shown that acute phorbol ester treatment increases the frequency of Ca 2+ oscillations induced by uncaging IP 3 (Bartlett et al, 2015).…”

Section: Ll Open Accesssupporting

confidence: 85%

IP3-Dependent Ca2+ Oscillations Switch into a Dual Oscillator Mechanism in the Presence of PLC-Linked Hormones

et al. 2020

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Ca 2+ oscillations that depend on inositol-1,4,5-trisphosphate (IP 3 ) have been ascribed to biphasic Ca 2+ regulation of the IP 3 receptor (IP 3 R) or feedback mechanisms controlling IP 3 levels in different cell types. IP 3 uncaging in hepatocytes elicits Ca 2+ transients that are often localized at the subcellular level and increase in magnitude with stimulus strength. However, this does not reproduce the broad baseline-separated global Ca 2+ oscillations elicited by vasopressin. Addition of hormone to cells activated by IP 3 uncaging initiates a qualitative transition from high-frequency spatially disorganized Ca 2+ transients, to low-frequency, oscillatory Ca 2+ waves that propagate throughout the cell. A mathematical model with dual coupled oscillators that integrates Ca 2+ -induced Ca 2+ release at the IP 3 R and mutual feedback mechanisms of cross-coupling between Ca 2+ and IP 3 reproduces this behavior. Thus, multiple Ca 2+ oscillation modes can coexist in the same cell, and hormonal stimulation can switch from the simpler to the more complex to yield robust signaling.

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Section: Ll Open Accesssupporting

confidence: 85%

IP3-Dependent Ca2+ Oscillations Switch into a Dual Oscillator Mechanism in the Presence of PLC-Linked Hormones

et al. 2020

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“…But the perception and transmission of the signal in the nucleoplasm is initiated by Ca 2+ release from the (1,4,5)InsP 3 -sensitive pools located in the nuclear cisternal membrane. A nuclear protein kinase can modify the nuclear cisternal (1,4,5)InsP 3 channel to increase its sensitivity to (1,4,5)InsP 3 (Matter et al 1993). Nuclear cisternal channels sensitive to cADP-R are also thought to be present (Perez-Terzic et al 1997).…”

Section: (A) the Nucleus And Regulation Of Gene Expressionmentioning

confidence: 99%

Spatial characteristics to calcium signalling; the calcium wave as a basic unit in plant cell calcium signalling

Malhó

Moutinho

Luit

et al. 1998

Phil. Trans. R. Soc. Lond. B

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Many signals that modify plant cell growth and development initiate changes in cytoplasmic Ca 2+ . The subsequent movement of Ca 2+ in the cytoplasm is thought to take place via waves of free Ca 2+ . These waves may be initiated at de¢ned regions of the cell and movement requires release from a reticulated endoplasmic reticulum and the vacuole. The mechanism of wave propagation is outlined, and the possible basis of repetitive wave formation, Ca 2+ oscillations and capacitative Ca 2+ signalling is discussed. Evidence for the presence of Ca 2+ waves in plant cells is outlined, and from studies on raphides it is suggested that the capabilities for capacitative Ca 2+ signalling are also present. The paper ¢nishes with an outline of the possible interrelation between Ca 2+ waves and organelles and describes the intercellular movement of Ca 2+ waves and the relevance of such information communication to plant development.

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“…. Certain isoforms of PKC have also been shown to translocate to the nuclear envelope upon activation, where they may regulate nuclear envelope breakdown or changes in gene expression that accompany a mitogenic response (Cambier et al, 1987;Huange et al, 1988;Thomas et al, 1988;Leach et al, 1989;Masmoudi et al, 1989;Fields et al, , 1990Rogue et al, 1990;Divecha et al, 1991;Hocevar and Fields, 1991;Block et al, 1992;Eldar et al, 1992;James and Olson, 1992;Matter et al, 1993).…”

mentioning

confidence: 99%

PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system.

Staudinger

Zhou

Burgess

et al. 1995

The Journal of Cell Biology

276

221

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Abstract. Protein kinase C (PKC) plays a central role in the control of proliferation and differentiation of a wide range of cell types by mediating the signal transduction response to hormones and growth factors. Upon activation by diacylglycerol, PKC translocates to different subcellular sites where it phosphorylates numerous proteins, most of which are unidentified. We used the yeast two-hybrid system to identify proteins that interact with activated PKCot. Using the catalytic region of PKC fused to the DNA binding domain of yeast GAL4 as "bait" to screen a mouse T cell cDNA library in which cDNA was fused to the GAL4 activation domain, we cloned several novel proteins that interact with C-kinase (PICKs). One of these proteins, designated PICK1, interacts specifically with the catalytic domain of PKC and is an efficient substrate for phosphorylation by PKC in vitro and in vivo. PICK1 is localized to the perinuclear region and is phosphorylated in response to PKC activation. PICK1 and other PICKs may play important roles in mediating the actions of PKC.

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Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei.

Cited by 127 publications

References 34 publications

IP3-Dependent Ca2+ Oscillations Switch into a Dual Oscillator Mechanism in the Presence of PLC-Linked Hormones

IP3-Dependent Ca2+ Oscillations Switch into a Dual Oscillator Mechanism in the Presence of PLC-Linked Hormones

Spatial characteristics to calcium signalling; the calcium wave as a basic unit in plant cell calcium signalling

PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system.

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