Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions.

@article{Wang2002LateralSO,
  title={Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions.},
  author={Jiyao Wang and Alok Gambhir and Gy{\"o}ngyi Hangy{\'a}s-Mih{\'a}lyn{\'e} and Diana Murray and Urszula P. Golebiewska and Stuart McLaughlin},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 37},
  pages={34401-12}
}
A peptide corresponding to the basic (+13), unstructured effector domain of myristoylated alanine-rich C kinase substrate (MARCKS) binds strongly to membranes containing phosphatidylinositol 4,5-bisphosphate (PIP(2)). Although aromatic residues contribute to the binding, three experiments suggest the binding is driven mainly by nonspecific local electrostatic interactions. First, peptides with 13 basic residues, Lys-13 and Arg-13, bind to PIP(2)-containing vesicles with the same high affinity… CONTINUE READING

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