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Sci. Signal., 7 February 2012
Vol. 5, Issue 210, p. ra11
Regulating Zinc Signals
Zinc, which has emerged as a second messenger, is released from intracellular stores, leading to activation of tyrosine kinases and thereby to stimulation of pathways involved in cell proliferation and migration. Here, Taylor et al. uncover evidence implicating the kinase CK2, which plays a prominent role in cell proliferation, in this process through its association with and phosphorylation of the endoplasmic reticulum–resident zinc channel ZIP7. Inhibition of CK2 attenuated zinc release from the endoplasmic reticulum and downstream signals. A functional mutation of ZIP7 that interfered with CK2-ZIP7 interactions prevented ZIP7-mediated zinc signals, decreased downstream signaling events, and attenuated ZIP7-mediated cell migration. Thus, the authors conclude that CK2 plays a crucial role in the activation of ZIP7 and thereby in mediating zinc signals.
Citation: K. M. Taylor, S. Hiscox, R. I. Nicholson, C. Hogstrand, P. Kille, Protein Kinase CK2 Triggers Cytosolic Zinc Signaling Pathways by Phosphorylation of Zinc Channel ZIP7. Sci. Signal.5, ra11 (2012).
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