Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles.

@article{Kim1994PhosphorylationHI,
  title={Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles.},
  author={Junhyong Kim and Tetsuya Shishido and Xuejun Jiang and Alan Aderem and Stuart McLaughlin},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 45},
  pages={28214-9}
}
The myristoylated alanine-rich protein kinase C substrate (MARCKS) is a major cellular substrate of protein kinase C (PKC), and PKC phosphorylation produces translocation of MARCKS from membrane to cytoplasm in many cells. Our working hypothesis is that binding of MARCKS to biological membranes requires both hydrophobic insertion of its myristoyl chain into the lipid bilayer and electrostatic interaction of its basic domain with acidic lipids. We tested this hypothesis by measuring the binding… CONTINUE READING

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