Pik1-ing clathrin adaptors

Nat Cell Biol. 2012 Feb 19;14(3):231-2. doi: 10.1038/ncb2448.

Abstract

Clathrin adaptor proteins are essential for clathrin-coated vesicle biogenesis, yet the mechanisms governing their recruitment and interactions remain incompletely defined. The clathrin adaptors Gga and AP-1 are now shown to be recruited sequentially to the trans-Golgi network in two waves of clathrin coat assembly, coupled by Pik1-mediated phosphatidylinositol-4-phosphate synthesis. These findings reveal mechanistic insights into the functional and regulatory relationships between these clathrin adaptors.

Publication types

  • Comment

MeSH terms

  • 1-Phosphatidylinositol 4-Kinase / metabolism*
  • Adaptor Proteins, Vesicular Transport / metabolism*
  • Phosphatidylinositol Phosphates / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • trans-Golgi Network / metabolism*

Substances

  • Adaptor Proteins, Vesicular Transport
  • Gga2 protein, S cerevisiae
  • Phosphatidylinositol Phosphates
  • Saccharomyces cerevisiae Proteins
  • phosphatidylinositol 4-phosphate
  • 1-Phosphatidylinositol 4-Kinase
  • PIK1 protein, S cerevisiae