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Terminal deoxynucleotidil transferase is a nuclear PKC substrate
O Trubiani1, F J Bollum, R Di Primio
1Istituto di Morfologia Umana Normale, Facoltà di Medicina, Università di Chieti, Italy.
FEBS Letters
|November 6, 1995
Summary
Terminal deoxynucleotidyl transferase (TdT) is phosphorylated by Protein Kinase C (PKC). This suggests TdT phosphorylation regulates gene transcription and protein synthesis in lymphoid cells.
Area of Science:
- Molecular Biology
- Cellular Signaling
Background:
- Protein phosphorylation regulates cellular events in response to metabolic and environmental changes.
- Both Protein Kinase C (PKC) and Terminal deoxynucleotidyl transferase (TdT) levels are regulated by Phorbol 12-myristate 13-acetate (PMA).
Purpose of the Study:
- To investigate TdT phosphorylation in vivo and in vitro.
- To determine if PKC phosphorylates TdT.
Main Methods:
- Utilized KM-3 cells, a TdT-positive human pre-B cell line, treated with PMA for in vivo studies.
- Employed purified PKC and human recombinant TdT for in vitro studies.
Main Results:
- Demonstrated that TdT is a substrate for PKC activity.
- Confirmed TdT phosphorylation by PKC.
Conclusions:
- TdT phosphorylation by PKC may play a key role in regulating gene transcription and protein synthesis.
- This phosphorylation event is potentially significant during lymphoid cell differentiation.