|Title:||Determination of the structural requirements for palmitoylation of p63|
|Authors :||Schweizer, Anja|
|Published in :||Journal of Biological Chemistry|
|Publisher / Ed. Institution :||American Society for Biochemistry and Molecular Biology|
|License (according to publishing contract) :||Licence according to publishing contract|
|Type of review:||Peer review (Publication)|
|Subject (DDC) :||572: Biochemistry|
|Abstract:||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 [3H]palmitate, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis. By investigating deletion and point mutations, Cys100 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 Cys100 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.|
|Departement:||Life Sciences und Facility Management|
|Publication type:||Article in scientific Journal|
|Appears in Collections:||Publikationen Life Sciences und Facility Management|
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