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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Thyrotropin-stimulated phosphorylation of high mobility group protein 14 in vivo at the site catalyzed by cyclic nucleotide-dependent protein kinases in vitro.

Thyrotropin (TSH) treatment of bovine thyroid slices increased 32P-labeling of chromosomal high mobility group 14 (HMG) protein approximately 2-fold. Analogs of cAMP, but not cGMP, also enhanced phosphorylation of HMG 14. The sites of phosphorylation were analyzed by partial acid hydrolysis and by two-dimensional mapping of tryptic digests of 32P-labeled HMG 14 which was purified from control and TSH-treated thyroid tissue. TSH treatment enhanced phosphorylation at serine residues in four prominent tryptic phosphopeptides which were identical with those derived from HMG 14 phosphorylated in vitro with cAMP- and cGMP-dependent protein kinases. The four tryptic phosphopeptides contain serine 6, the major site of in vitro phosphorylation catalyzed by cyclic nucleotide-dependent protein kinases (Walton, G. M., Spiess, J., and Gill, G. N. (1982) J. Biol. Chem. 257, 4661-4668). TSH did not affect phosphorylation of serine 24, a minor site of phosphorylation in vitro. These studies suggest that TSH-stimulated phosphorylation of HMG 14 is catalyzed by cAMP-dependent protein kinase.[1]

References

  1. Thyrotropin-stimulated phosphorylation of high mobility group protein 14 in vivo at the site catalyzed by cyclic nucleotide-dependent protein kinases in vitro. Walton, G.M., Gill, G.N., Cooper, E., Spaulding, S.W. J. Biol. Chem. (1984) [Pubmed]
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