Structural basis of dynamic membrane recognition by trans-Golgi network specific FAPP proteins.

@article{Lenoir2015StructuralBO,
  title={Structural basis of dynamic membrane recognition by trans-Golgi network specific FAPP proteins.},
  author={Marc Lenoir and Michał Grzybek and Michał Majkowski and Sandya Chinna Rajesh and Jaswant Singh Varinder Kaur and Sara B-M Whittaker and {\"U}nal Coskun and Michael Overduin},
  journal={Journal of molecular biology},
  year={2015},
  volume={427 4},
  pages={
          966-981
        }
}
Glycosphingolipid metabolism relies on selective recruitment of the pleckstrin homology (PH) domains of FAPP proteins to the trans-Golgi network. The mechanism involved is unclear but requires recognition of phosphatidylinositol-4-phosphate (PI4P) within the Golgi membrane. We investigated the molecular basis of FAPP1-PH domain interactions with PI4P bilayers in liposome sedimentation and membrane partitioning assays. Our data reveals a mechanism in which FAPP-PH proteins preferentially target… CONTINUE READING

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