Unusual structural organization of the endocytic proteins AP180 and epsin 1.

@article{Kalthoff2002UnusualSO,
  title={Unusual structural organization of the endocytic proteins AP180 and epsin 1.},
  author={Christoph Kalthoff and J{\"u}rgen Alves and Claus Urbanke and Ruth Knorr and Ernst J. Ungewickell},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 10},
  pages={8209-16}
}
Epsin and AP180/CALM are important endocytic accessory proteins that are believed to be involved in the formation of clathrin coats. Both proteins associate with phosphorylated membrane inositol lipids through their epsin N-terminal homology domains and with other components of the endocytic machinery through short peptide motifs in their carboxyl-terminal segments. Using hydrodynamic and spectroscopic methods, we demonstrate that the parts of epsin 1 and AP180 that are involved in protein… CONTINUE READING
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