Article
Amino acid substitution in NPC1 that abolishes cholesterol binding reproduces phenotype of complete NPC1 deficiency in mice.
Proceedings of the National Academy of Sciences of the United States of America - 13 Sept 2011
Xie Xuefen, Brown Michael S, Shelton John M, Richardson James A, Goldstein Joseph L, Liang Guosheng
Abstract excerpt
Substitution mutations in adjacent amino acids of the N-terminal domain of NPC1, a lysosomal membrane protein, abolish its cholesterol binding activity and impair its ability to export cholesterol from lysosomes of cultured cells lacking npc1 [Kwon HJ, et al. (2009) Cell 137:1213-1224]. Here, we show that the same two mutations (proline-202 and phenylalanine-203, both changed to alanine) reproduce the phenotype...
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