Global Analysis of Protein Palmitoylation in Yeast
| Autor: | Jason A. Kuchar, Amy F. Roth, John R. Yates, William N. Green, Junmei Wan, Aaron O. Bailey, Beimeng Sun, Brett S. Phinney, Nicholas G. Davis |
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| Jazyk: | angličtina |
| Předmět: |
Saccharomyces cerevisiae Proteins
Protein family Proteome Biochemistry Genetics and Molecular Biology(all) Palmitic Acid technology industry and agriculture S-acylation Saccharomyces cerevisiae Biology Protein lipidation General Biochemistry Genetics and Molecular Biology Article Cell biology Palmitoylation Biochemistry Acetyltransferases Mutation Protein palmitoylation lipids (amino acids peptides and proteins) Lipid modification Palmitoyl acyltransferase DHHC domain Protein Processing Post-Translational Acyltransferases Signal Transduction |
| Zdroj: | Cell. (5):1003-1013 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/j.cell.2006.03.042 |
| Popis: | SummaryProtein palmitoylation is a reversible lipid modification that regulates membrane tethering for key proteins in cell signaling, cancer, neuronal transmission, and membrane trafficking. Palmitoylation has proven to be a difficult study: Specifying consensuses for predicting palmitoylation remain unavailable, and first-example palmitoylation enzymes—i.e., protein acyltransferases (PATs)—were identified only recently. Here, we use a new proteomic methodology that purifies and identifies palmitoylated proteins to characterize the palmitoyl proteome of the yeast Saccharomyces cerevisiae. Thirty-five new palmitoyl proteins are identified, including many SNARE proteins and amino acid permeases as well as many other participants in cellular signaling and membrane trafficking. Analysis of mutant yeast strains defective for members of the DHHC protein family, a putative PAT family, allows a matching of substrate palmitoyl proteins to modifying PATs and reveals the DHHC family to be a family of diverse PAT specificities responsible for most of the palmitoylation within the cell. |
| Databáze: | OpenAIRE |
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