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Article Abstract
The regulation of insulin biosynthesis and secretion in pancreatic β-cells is essential for glucose homeostasis in humans. Previous findings point to the highly conserved, ubiquitously expressed serine/threonine kinase CK2 as having a negative regulatory impact on this regulation. In the cell culture model of rat pancreatic β-cells INS-1, insulin secretion is enhanced after CK2 inhibition. This enhancement is preceded by a rise in the cytosolic Ca concentration. Here, we identified the serine residues S and S of the voltage-dependent calcium channel Ca2.1 as targets of CK2 phosphorylation. Furthermore, co-immunoprecipitation experiments revealed that Ca2.1 binds to CK2 in vitro and in vivo. Ca2.1 knockdown experiments showed that the increase in the intracellular Ca concentration, followed by an enhanced insulin secretion upon CK2 inhibition, is due to a Ca influx through Ca2.1 channels. In summary, our results point to a modulating role of CK2 in the Ca2.1-mediated exocytosis of insulin.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7370021 | PMC |
| http://dx.doi.org/10.3390/ijms21134668 | DOI Listing |
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