Key result
Phorbol ester stimulation drives firmer PKC alpha association with nuclear components in neuroblastoma cells.
PKC alpha is constitutively present in the nucleoplasm of Neuro-2a cells and associates more firmly with nuclear components upon phorbol ester stimulation, suggesting it can phosphorylate nucleoplasmic proteins.
Nuclear PKCα stabilization in neuroblastoma cells is hypothesis-generating; leaves open relevance to cardiovascular signaling or therapy.
Using activity measurements and Western blotting, we demonstrated that PKC alpha is constitutively present in nuclei of Neuro-2a neuroblastoma cells. Confocal microscopy revealed that PKC alpha is present in the nucleoplasm and that this localization does not change after stimulation with phorbol ester. However, as revealed by extraction experiments, phorbol ester leads to a firmer association of PKC alpha with nuclear components. Our findings suggest that PKC alpha not only associates with lipids but also with proteins inside the nucleus. The presence of active PKC alpha inside the nucleus allows the enzyme to phosphorylate not only proteins at the nuclear envelope but also proteins in the nucleoplasm.
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Buchner et al. (1997) studied Neuroblastoma (Neuro-2a cells). Phorbol ester vs. Unstimulated cells was evaluated on Localization and association of PKC alpha with nuclear components. Phorbol ester stimulation of Neuro-2a neuroblastoma cells leads to a firmer association of constitutively nuclear PKC alpha with nuclear components, suggesting interaction with nuclear proteins.
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