• Biology, Medicine
  • Published in
    The Journal of biological…
    1994

Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein.

@article{Verghese1994ProteinKC,
  title={Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein.},
  author={George M. Verghese and James D. Johnson and C Vasulka and Dale M. Haupt and Deborah J. Stumpo and Perry J. Blackshear},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 12},
  pages={
          9361-7
        }
}
The myristoylated alanine-rich C kinase substrate (MARCKS) and the MARCKS-related protein (MRP) are members of a distinct family of protein kinase C (PKC) substrates that also bind calmodulin in a manner regulated by phosphorylation by PKC. The kinetics of PKC-mediated phosphorylation and the calmodulin binding properties of intact, recombinant MARCKS and MRP were investigated and compared with previous studies of synthetic peptides spanning the PKC phosphorylation site/calmodulin binding… CONTINUE READING

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