Calcium, protease action, and the regulation of the cell cycle

Santella, Luigia; Kyozuka, Keiichiro; Riso, Laura De; Carafoli, Ernesto

doi:10.1016/s0143-4160(98)90110-5

Cited by 74 publications

(49 citation statements)

References 44 publications

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“…The activation of proteasome by increased action potentials required external calcium influx through NMDA receptors and L-type VGCCs. UPS components may be regulated directly by Ca 2ϩ (65)(66)(67)(68), and it has been reported that the release of Ca 2ϩ from intracellular stores transiently activates the 26 S proteasome (69). Our findings are in line with these studies, and they provide evidence for Ca 2ϩ signaling in the regulation of the proteasome activity in neurons.…”

Section: Discussionsupporting

confidence: 91%

Regulation of the Proteasome by Neuronal Activity and Calcium/Calmodulin-dependent Protein Kinase II

Djakovic

Schwarz

Baryłko

et al. 2009

Journal of Biological Chemistry

212

213

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Protein degradation via the ubiquitin proteasome system has been shown to regulate changes in synaptic strength that underlie multiple forms of synaptic plasticity. It is plausible, therefore, that the ubiquitin proteasome system is itself regulated by synaptic activity. By utilizing live-cell imaging strategies we report the rapid and dynamic regulation of the proteasome in hippocampal neurons by synaptic activity. We find that the blockade of action potentials (APs) with tetrodotoxin inhibited the activity of the proteasome, whereas the up-regulation of APs with bicuculline dramatically increased the activity of the proteasome. In addition, the regulation of the proteasome is dependent upon external calcium entry in part through N-methyl-D-aspartate receptors and L-type voltage-gated calcium channels and requires the activity of calcium/calmodulindependent protein kinase II (CaMKII). Using in vitro and in vivo assays we find that CaMKII stimulates proteasome activity and directly phosphorylates Rpt6, a subunit of the 19 S (PA700) subcomplex of the 26 S proteasome. Our data provide a novel mechanism whereby CaMKII may regulate the proteasome in neurons to facilitate remodeling of synaptic connections through protein degradation.

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Section: Discussionsupporting

confidence: 91%

Regulation of the Proteasome by Neuronal Activity and Calcium/Calmodulin-dependent Protein Kinase II

Djakovic

Schwarz

Baryłko

et al. 2009

Journal of Biological Chemistry

212

213

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“…This phenomenon of relocation of proteins, such as p34 cdc2 -cyclin B complex (Ookata et al, 1992) and calpain (Santella et al, 1998), to the nucleus has been observed before GVBD in starfish oocyte. The link between these molecules and meiosis has to be further investigated.…”

Section: Involvement Of Plc-␤1 In the Meiotic Resumption Processmentioning

confidence: 61%

“…The 100-kDa fragment lacking the C-terminal region necessary for nuclear translocation (Kim et al, 1996) seems unable to move from the cytoplasm into the nucleus. And calpain has been found in the GV of the starfish (Santella et al, 1998) and rat (Malcov et al, 1997) oocytes, where it is predominantly present just before GVBD (Santella et al, 1998).…”

Section: Dynamics Of the Plc-␤1 Subcellular Locationmentioning

confidence: 99%

“…Nevertheless, the only fragment detected in the mouse oocyte subcellular fractions not treated with calpain inhibitors was the 100-kDa proteolytic fragment of PLC-␤1a. This could be due to an accumu-lation of calpain in the GV before GVBD, as in the starfish oocytes (Santella et al, 1998). This fragment, which is as catalytically active as the intact enzyme (Rhee et al, 1989;Wu et al, 1993), is not activated by the G-protein ␣q subunit (Park et al, 1993).…”

Section: Involvement Of Plc-␤1 In the Meiotic Resumption Processmentioning

confidence: 99%

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Cytoplasmic and Nuclear Phospholipase C-β1 Relocation: Role in Resumption of Meiosis in the Mouse Oocyte

Avazeri

Courtot

Pesty

et al. 2000

MBoC

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The location of the phospholipase C β1-isoform (PLC-β1) in the mouse oocyte and its role in the resumption of meiosis were examined. We used specific monoclonal antibodies to monitor the in vitro dynamics of the subcellular distribution of the enzyme from the release of the oocyte from the follicle until breakdown of the germinal vesicle (GVBD) by Western blotting, electron microscope immunohistochemistry, and confocal microscope immunofluorescence. PLC-β1 became relocated to the oocyte cortex and the nucleoplasm during the G2/M transition, mainly in the hour preceding GVBD. The enzyme was a 150-kDa protein, corresponding to PLC-β1a. Its synthesis in the cytoplasm increased during this period, and it accumulated in the nucleoplasm. GVBD was dramatically inhibited by the microinjection of anti-PLC-β1 monoclonal antibody into the germinal vesicle (GV) only when this accumulation was at its maximum. In contrast, PLC-γ1 was absent from the GV from the time of release from the follicle until 1 h later, and microinjection of anti-PLC-γ1 into the GV did not affect GVBD. Our results demonstrate a relationship between the relocation of PLC-β1 and its role in the first step of meiosis.

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“…In support of this, calpain has been shown to cleave many adhesion plaque proteins, such as talin, ezrin, pp125 FAK , and the cytoplasmic tail of ␤ 1 and ␤ 3 integrins (7-13). However, calpain does cleave other cytosolic and nuclear targets (14) and is involved in other responses such as proliferation and apoptosis (15)(16)(17)(18)(19).…”

mentioning

confidence: 99%

Membrane Proximal ERK Signaling Is Required for M-calpain Activation Downstream of Epidermal Growth Factor Receptor Signaling

Glading

Überall

Keyse

et al. 2001

Journal of Biological Chemistry

188

165

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Localization of signaling is critical in directing cellular outcomes, especially in pleiotropic signaling pathways. The extracellular signal-regulated kinase (ERK)/ microtubule-associated protein kinase, which promotes cell migration, proliferation, and differentiation is found in the nucleus and throughout the cytoplasm. Recently, it has been shown that nuclear translocation of ERK is required for transcriptional changes and cell proliferation. However, the cellular consequences, of cytoplasmic signaling have not been defined. We explored whether cytoplasmic, specifically membrane-proximal, ERK signaling is involved in growth factor-induced cell motility. We previously have demonstrated that increased M-calpain activity downstream of epidermal growth factor receptor (EGFR)-mediated ERK activation is necessary for epidermal growth factor (EGF)-induced motility. Calpain isoforms also have been found in nuclear, cytosolic, and plasma membrane-associated compartments in a variety of cell types. We now employ cell engineering approaches to control localization of the upstream EGFR and ERK activities to examine the spatial effect of upstream signal locale on downstream calpain activity. With differential ligand-induced internalization and trafficking-restricted receptor variants, we find that calpain activity is triggered only by plasma membrane-restricted activated EGFR, not by internalized (although still active) EGFR. Cells transfected with membrane-targeted ERK1 and ERK2, which sequester endogenous ERKs, exhibited normal EGF-induced calpain activity. Transfection of an inactive ERK phosphatase (MKP-3/Pyst1) that sequesters ERK in the cytoplasm prevented calpain activation as well as deadhesion. These data strongly suggest that EGF-induced calpain activity can be enhanced near sites of membrane-proximal EGFR-mediated ERK signaling, providing insights about how calpain activity might be regulated and targeted to enhance its effects on adhesionrelated substrates.

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Calcium, protease action, and the regulation of the cell cycle

Cited by 74 publications

References 44 publications

Regulation of the Proteasome by Neuronal Activity and Calcium/Calmodulin-dependent Protein Kinase II

Regulation of the Proteasome by Neuronal Activity and Calcium/Calmodulin-dependent Protein Kinase II

Cytoplasmic and Nuclear Phospholipase C-β1 Relocation: Role in Resumption of Meiosis in the Mouse Oocyte

Membrane Proximal ERK Signaling Is Required for M-calpain Activation Downstream of Epidermal Growth Factor Receptor Signaling

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