Interaction of autophosphorylated Ca2+/calmodulin-dependent protein kinase II with neuronal cytoskeletal proteins. Characterization of binding to a 190-kDa postsynaptic density protein.

@article{McNeill1995InteractionOA,
  title={Interaction of autophosphorylated Ca2+/calmodulin-dependent protein kinase II with neuronal cytoskeletal proteins. Characterization of binding to a 190-kDa postsynaptic density protein.},
  author={R. Blair McNeill and Roger J Colbran},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 17},
  pages={10043-9}
}
Subcellular localization of Ca2+/calmodulin-dependent protein kinase II (CaMKII) by interaction with specific anchoring proteins may be an important mechanism contributing to the regulation of CaMKII. Proteins capable of binding CaMKII were identified by the use of a gel overlay assay with recombinant mouse CaMKII alpha (mCaMKII alpha) or Xenopus CaMKII beta (xCaMKII beta) 32P-autophosphorylated at Thr286/287 as a probe. Numerous [32P]CaMKII-binding proteins were identified in various whole rat… CONTINUE READING
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