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• W1988093399 abstract "Lamin B was shown to be a major substrate of cellular phosphorylation in the response of lymphocytes to phorbol esters. Lamins A and C, which were not observed in lymphocytes, were also substrates of phorbol-stimulated phosphorylation in those cell types that express them. Lamin B phosphopeptides labeled with 32P in intact cells treated with phorbol 12-myristate 13-acetate were compared to those produced by in vitro phosphorylation with protein kinase M, cAMP-dependent protein kinase, and Ca2+/calmodulin-dependent protein kinase II. The phosphopeptides labeled by in vivo stimulation with phorbol esters are very similar to those phosphorylated in vitro by protein kinase M, a catalytic domain of protein kinase C. Phorbol treatment of interphase cells significantly reduces the amount of detergent-insoluble lamin B, suggesting that phosphorylation of lamin may alter the architecture of the nuclear lamina. In addition, we have shown that treatment of a B-cell line with antibodies to IgM induces a modest increase in lamin B phosphorylation. These results strongly suggest that ligands that are known to activate protein kinase C at the cell surface or in the cytosol also lead to the activation of a nuclear kinase activity with a protein kinase C-type specificity." @default.
• W1988093399 created "2016-06-24" @default.
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• W1988093399 date "1988-04-01" @default.
• W1988093399 modified "2023-10-17" @default.
• W1988093399 title "Lamin B is rapidly phosphorylated in lymphocytes after activation of protein kinase C." @default.
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• W1988093399 doi "https://doi.org/10.1073/pnas.85.7.2279" @default.
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