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Related Experiment Videos

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
PubMed
Summary
This summary is machine-generated.

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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.

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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.