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. 1988 Apr;85(7):2279–2283. doi: 10.1073/pnas.85.7.2279

Lamin B is rapidly phosphorylated in lymphocytes after activation of protein kinase C.

P Hornbeck 1, K P Huang 1, W E Paul 1
PMCID: PMC279974  PMID: 3353377

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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