Protein kinase CK2 opens the gate for zinc signaling - PubMed (original) (raw)

Editorial

. 2012 May 15;11(10):1863-4.

doi: 10.4161/cc.20414. Epub 2012 May 15.

• PMID: 22580452
• PMCID: PMC3359116
• DOI: 10.4161/cc.20414

Editorial

Protein kinase CK2 opens the gate for zinc signaling

Kathryn M Taylor et al. Cell Cycle. 2012.

No abstract available

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Figures

Figure 1. Schematic illustration of the second messenger signaling pathway proposed for Zn2+. Various external stimuli cause protein kinase CK2 to phosphorylate endoplasmic reticulum (ER) located zinc transporter, ZIP7 which causes the gated release of Zn2+ stored within the ER through the ZIP7 channel to create a cytosolic ‘zinc wave’. After phosphorylating its target CK2 dissociates from ZIP7 and may move into the nucleus. We postulate that elevated Zn2+ within the cytosol may selectively inhibit tyrosine phosphatases leading to prolonged tyrosine kinase activation and an observed downstream increase in pERK and pAKT resulting in cell proliferation and migration. These events, representing a short-term second messenger activity for Zn, completing within a 20 min time period, are thus temporally separated from established transcriptional impact of zinc ions which is mediated by metal transcription factor-1 (MTF-1) and is known to regulate metallothionein (MT), glutamylcysteine synthetase (GCS) and ZnT1 (SLC30A1).

Comment in

• Taylor KM, Hiscox S, Nicholson RI, Hogstrand C, Kille P. Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. Sci Signal. 2012;5:ra11–ra11. doi: 10.1126/scisignal.2002585.

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