Title: Determination of the structural requirements for palmitoylation of p63
Authors : Schweizer, Anja
Rohrer, Jack
Kornfeld, Stuart
Published in : Journal of Biological Chemistry
Volume(Issue) : 270
Issue : 16
Pages : 9638
Pages to: 9644
Publisher / Ed. Institution : American Society for Biochemistry and Molecular Biology
Issue Date: 21-Apr-1995
License (according to publishing contract) : Licence according to publishing contract
Type of review: Peer review (Publication)
Language : English
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
DOI : 10.1074/jbc.270.16.9638
ISSN: 1083-351X
URI: https://digitalcollection.zhaw.ch/handle/11475/6802
Appears in Collections:Publikationen Life Sciences und Facility Management

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