The NECAP PHear domain increases clathrin accessory protein binding potential.

@article{Ritter2007TheNP,
  title={The NECAP PHear domain increases clathrin accessory protein binding potential.},
  author={Brigitte Ritter and Alexei Yu Denisov and Jacynthe Philie and Patrick D Allaire and Valerie Legendre-Guillemin and Peter Zylbergold and Kalle Gehring and Peter S McPherson},
  journal={The EMBO journal},
  year={2007},
  volume={26 18},
  pages={4066-77}
}
AP-2 is a key regulator of the endocytic protein machinery driving clathrin-coated vesicle (CCV) formation. One critical function, mediated primarily by the AP-2 alpha-ear, is the recruitment of accessory proteins. NECAPs are alpha-ear-binding proteins that enrich on CCVs. Here, we have solved the structure of the conserved N-terminal region of NECAP 1, revealing a unique module in the pleckstrin homology (PH) domain superfamily, which we named the PHear domain. The PHear domain binds accessory… CONTINUE READING
Highly Cited
This paper has 20 citations. REVIEW CITATIONS