. Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain. Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12473-8. PubMed.

Recommends

Please login to recommend the paper.

Comments

Make a Comment

To make a comment you must login or register.

Comments on Primary Papers and News

  1. Fascinating and a clear milestone. This will most likely trigger the discovery of many more cholesterol-sensing proteins and will greatly assist the understanding of the cell biology of the lipid-protein crossroads.

    View all comments by Tobias Hartmann
  2. Because of the accumulation of cholesterol in NPC patients having mutated NPC1, it has been assumed for many years that NPC1 is a cholesterol transporter. For the first time, the work of Ohgami et al. demonstrates a direct interaction between a cholesterol analog and NPC1 that requires the sterol-sensing domain of the protein. This is an important development in the field of NPC research. It opens the way to establishing similar functional interactions between other lipids and NPC1, and also NPC1-related proteins.

    View all comments by Inez Vincent
  3. This is an interesting paper in the cholesterol field. I can only agree with Tobias and Inez Vincent that the identification of the NPC1 sterol-sensing domain as a possible binding site for cholesterol may lead to new clues for protein-lipid interactions.

    View all comments by Dora M. Kovacs

This paper appears in the following:

News

  1. Caught in the Act: NPC1 Found to Bind Cholesterol