UV-light induces p38 MAPK-dependent phosphorylation of Bcl10

Biochem Biophys Res Commun. 2003 Feb 21;301(4):923-6. doi: 10.1016/s0006-291x(03)00063-9.


Bcl10 is a signaling protein required for activation of the NF-kappaB transcription factor. NF-kappaB is an important mediator of genotoxic stress and regulates the expression of genes required for both cell proliferation and cell death. Bcl10 is phosphorylated in vivo, however, the protein kinase or kinases responsible are not known. Here, we show that Bcl10 is phosphorylated in response to UV irradiation. UV-induced phosphorylation of Bcl10 was inhibited by the p38 stress-activated protein kinase inhibitors SB203580 and PD169316, suggesting that p38 is required for UV-mediated phosphorylation of Bcl10.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • B-Cell CLL-Lymphoma 10 Protein
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Cell Line
  • Dose-Response Relationship, Radiation
  • Enzyme Inhibitors / pharmacology
  • HeLa Cells
  • Humans
  • Imidazoles / pharmacology
  • MAP Kinase Signaling System / drug effects
  • MAP Kinase Signaling System / radiation effects
  • Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • Mitogen-Activated Protein Kinases / metabolism*
  • Mitogen-Activated Protein Kinases / radiation effects*
  • Phosphorylation
  • Pyridines / pharmacology
  • Tumor Cells, Cultured
  • Ultraviolet Rays
  • p38 Mitogen-Activated Protein Kinases


  • Adaptor Proteins, Signal Transducing
  • B-Cell CLL-Lymphoma 10 Protein
  • BCL10 protein, human
  • Carrier Proteins
  • Enzyme Inhibitors
  • Imidazoles
  • Pyridines
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • 2-(4-nitrophenyl)-4-(4-fluorophenyl)-5-(4-pyridinyl)-1H-imidazole
  • SB 203580