Mutagenesis of the regulatory subunit (RII beta) of cAMP-dependent protein kinase II beta reveals hydrophobic amino acids that are essential for RII beta dimerization and/or anchoring RII beta to the cytoskeleton.

@article{Li1995MutagenesisOT,
  title={Mutagenesis of the regulatory subunit (RII beta) of cAMP-dependent protein kinase II beta reveals hydrophobic amino acids that are essential for RII beta dimerization and/or anchoring RII beta to the cytoskeleton.},
  author={Ying Li and Charles S. Rubin},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 4},
  pages={1935-44}
}
In neurons cAMP-dependent protein kinase II beta (PKAII beta) is sequestered in the dendritic cytoskeleton because the regulatory subunit (RII beta) of the enzyme is tightly bound by A Kinase Anchor Proteins (AKAPs). The prototypic neuronal anchor protein AKAP75 has a COOH-terminal 22-residue RII beta binding (tethering) site. A key feature of the tethering site is that several amino acids with large aliphatic side chains mediate the high-affinity binding of RII beta. Mutagenesis, recombinant… CONTINUE READING

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