Changes of Nuclear PI-PLC γ1 During Rat Liver Regeneration

Neri, Luca M.; Ricci, Daniele; Carini, Cinzia; Marchisio, Marco; Capitani, Silvano; Bertagnolo, Valeria

doi:10.1016/s0898-6568(96)00178-7

Cited by 37 publications

(35 citation statements)

References 44 publications

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“…The differential subcellular localizations in normal or highly transformed cell lines might reflect the degree of transformation of the cell type or phase of the cell cycle (Diakonova et al, 1997). This idea is consistent with the observation of an increased amount of PLC-γ1 in the nuclei of regenerating rat liver at 22 hours, which suggests that there is a relationship between the S-phase of the cell cycle and intranuclear localization of PLC-γ1 (Neri et al, 1997). These results are supported by the findings that the levels of nuclear PtdIns lipids decrease by over 50% at 2 hours and 4 hours after release from the G1/S boundary (S-phase of the cell cycle) and return to their original levels by 9 hours, whereas the levels of the cytoplasmic PtdIns lipids remain constant throughout this period.…”

Section: Pike-s In Nuclear Pi 3-kinase Regulationsupporting

confidence: 91%

PIKE GTPase: a novel mediator of phosphoinositide signaling

Snyder

2004

Journal of Cell Science

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Phosphoinositide (PI) 3-kinase enhancer (PIKE) is a brain-specific GTPase that binds to PI 3-kinase and stimulates its lipid kinase activity. It exists in two forms: the first to be identified, PIKE-S, is shorter and exclusively nuclear; by contrast, the longer form, PIKE-L, resides in multiple intracellular compartments. Nerve growth factor treatment leads to PIKE-S activation by triggering the nuclear translocation of phospholipase C (PLC)-γ1, which acts as a physiological guanine nucleotide exchange factor (GEF) for PIKE-S through its Src-homlogy 3 (SH3) domain. Cytoplasmic PI 3-kinase and its lipid product phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P3] regulate the membrane translocation and activation of many signaling molecules by binding to their pleckstrin homology (PH) domains. However, little is known about the physiological roles of their nuclear counterparts. The nuclear PLC-γ1/PIKE-S/PI 3-kinase signaling pathway seems to be an extension of the crosstalk between cytoplasmic PLC-γ1 and PI 3-kinase. PIKE-L contains a C-terminal extension consisting of an ADP ribosylation-GTPase-activating protein (ArfGAP) domain and two ankyrin repeats in addition to the N-terminal GTPase domain. PIKE-L could have additional, extranuclear functions, including regulation of postsynaptic signaling by metabotropic glutamate receptors.

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Section: Pike-s In Nuclear Pi 3-kinase Regulationsupporting

confidence: 91%

PIKE GTPase: a novel mediator of phosphoinositide signaling

Snyder

2004

Journal of Cell Science

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“…The enzymatic machinery that hydrolyzes PIP 2 has been shown to be present in the nucleus also, suggesting that it may be involved in second messenger production within this cell compartment (11)(12)(13)(14)(15). Treatment of Swiss 3T3 cells with IGF-I led to a sustained increase in intranuclear DAG and a decrease in the levels of PIP and PIP 2 , whereas whole-cell levels of DAG showed no changes.…”

mentioning

confidence: 99%

Nuclear Diacylglycerol Produced by Phosphoinositide-specific Phospholipase C Is Responsible for Nuclear Translocation of Protein Kinase C-α

Neri

Borgatti²,

Capitani³

et al. 1998

Journal of Biological Chemistry

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It is well established that an independent inositide cycle is present within the nucleus, where it is involved in the control of cell proliferation and differentiation. Previous results have shown that when Swiss 3T3 cells are treated with insulin-like growth factor-I (IGF-I) a rapid and sustained increase in mass of diacylglycerol (DAG) occurs within the nuclei, accompanied by a decrease in the levels of both phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate. However, it is unclear whether or not other lipids could contribute to this prolonged rise in DAG levels. We now report that

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“…This behaviour indicates the presence of at least two different isoforms that are quantitatively different between the two fractions. The presence of two isoforms, beta1 in the chromatin and gamma1 in both the nuclear membrane and chromatin fractions, were demonstrated using specific antibodies coupled with electron microscopy (Neri et al 1997). However, the delta1 isoform that is present in the cytoplasm was absent from the nuclei.…”

Section: Phosphatidylinositol-dependent Phospholipase Cmentioning

confidence: 99%