Terminal deoxynucleotidil transferase is a nuclear PKC substrate.
Protein phosphorylation is the regulatory mechanism of many cellular events in response to changes in metabolic activity and environmental conditions. Seeing that PKC and TdT levels in cells are both regulated by PMA, we sought particularly intriguing to investigate TdT phosphorylation in vivo, utilizing KM-3 cells, a TdT-positive human pre-B cell line treated with PMA and in vitro, employing purified PKC and human recombinant TdT. Our data show that TdT is a substrate for PKC activity, suggesting that TdT phosphorylation could play a key role in the pathway affecting the control of gene transcription and protein synthesis during lymphoid cells differentiation.
Trubiani
O
O
Istituto di Morfologia Umana Normale, Facoltà di Medicina, Università di Chieti, Italy.
Bollum
F J
FJ
Di Primio
R
R
D001345:Autoradiography; D001402:B-Lymphocytes / Q000201:enzymology; D015153:Blotting, Western; D002467:Cell Nucleus / Q000201:enzymology*; D004253:DNA Nucleotidylexotransferase / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D011994:Recombinant Proteins; D011493:Protein Kinase C; D004253:DNA Nucleotidylexotransferase; D013755:Tetradecanoylphorbol Acetate