DETERMINATION OF THE STRUCTURAL REQUIREMENTS FOR PALMITOYLATION OF P63

被引:37
作者
SCHWEIZER, A
ROHRER, J
KORNFELD, S
机构
[1] Department of Medicine, Washington Univ. School of Medicine, St. Louis
关键词
D O I
10.1074/jbc.270.16.9638
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Palmitoylation of p63, a type II membrane protein localized in the endoplasmic reticulum, is induced in a reversible manner by the drug brefeldin A. To study the requirements for palmitoylation, mutant forms of p63 were expressed in COS cells and analyzed by metabolic labeling with [H-3]palmitate, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis. By investigating deletion and point mutations, Cys(100) in the 106-amino acid cytoplasmic tail of p63 has been identified as the site of acylation. Site directed mutagenesis of residues 99-105 together with cytoplasmic tail truncation mutants showed that the amino acids surrounding Cys(100) are not critical for palmitoylation of this residue. Analysis of a chimeric construct between p63 and the plasma membrane protein dipeptidylpeptidase IV further revealed that p63 palmitoylation is not dependent on its transmembrane domain. In contrast, the six-amino acid distance between the end of the predicted transmembrane domain and the palmitoylation site was found to be essential for proper acylation of p63.
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页码:9638 / 9644
页数:7
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