Regulation of the Src family kinase Lck by Hsp90 and ubiquitination.

@article{Giannini2004RegulationOT,
  title={Regulation of the Src family kinase Lck by Hsp90 and ubiquitination.},
  author={Ana Lucia Giannini and Marie-Jos{\'e} Bijlmakers},
  journal={Molecular and cellular biology},
  year={2004},
  volume={24 13},
  pages={5667-76}
}
Regulation of the Src-related tyrosine kinase Lck is crucial to the outcome of T-cell receptor (TCR) stimulation. It was previously shown that the stability of the constitutively active mutant LckY505F is controlled by Hsp90 (M. J. Bijlmakers and M. Marsh, Mol. Biol. Cell. 11:1585-1595, 2000). Here we establish that following TCR stimulation, endogenous activated Lck in T cells is also degraded in the presence of the Hsp90 inhibitor geldanamycin. Using Lck constructs expressed in COS-7 cells… CONTINUE READING

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