Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis.

@article{Singh2003IdentificationOT,
  title={Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis.},
  author={Saurabh P. Singh and David W. Powell and Madhavi J. Rane and Tom H Millard and John O. Trent and William M. Pierce and Jon B. Klein and Laura M Machesky and Kenneth R Mcleish},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 38},
  pages={
          36410-7
        }
}
The p38 MAPK pathway regulates multiple neutrophil functional responses via activation of the serine-threonine kinase MAPK-activated protein kinase 2 (MAPKAPK2). To identify substrates of MAPKAPK2 that mediate these responses, a proteomic approach was used in which in vitro phosphorylation of neutrophil lysates by exogenously added active recombinant MAPKAPK2 was followed by protein separation using two-dimensional electrophoresis. Peptide mass fingerprinting of peptides defined by MALDI-MS was… CONTINUE READING
BETA

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 25 CITATIONS

Similar Papers

Loading similar papers…