Palmitoylation: a protein S-acylation with implications for breast cancer
Open Access
- 19 October 2016
- journal article
- review article
- Published by Springer Science and Business Media LLC in npj Breast Cancer
- Vol. 2 (1), 16028
- https://doi.org/10.1038/npjbcancer.2016.28
Abstract
Protein S-acylation is a reversible post-translational lipid modification that involves linkage of a fatty acid chain predominantly to a cysteine amino acid via a thioester bond. The fatty acid molecule is primarily palmitate, thus the term ‘palmitoylation’ is more commonly used. Palmitoylation has been found to modulate all stages of protein function including maturational processing, trafficking, membrane anchoring, signaling range and efficacy, and degradation. In breast cancer, palmitoylation has been shown to control the function of commonly dysregulated genes including estrogen receptors, the epidermal growth factor (EGF) family of receptors, and cancer stem cell markers. Importantly, palmitoylation is a critical factor controlling the formation of complexes at the plasma membrane involving tetraspanins, integrins, and gene products that are key to cell–cell communication. During metastasis, cancer cells enhance their metastatic capacity by interacting with stroma and immune cells. Although aberrant palmitoylation could contribute to tumor initiation and growth, its potential role in these cell–cell interactions is of particular interest, as it may provide mechanistic insight into metastasis, including cancer cell-driven immune modulation. Compelling evidence for a role for aberrant palmitoylation in breast cancer remains to be established. To this end, in this review we summarize emerging evidence and highlight pertinent knowledge gaps, suggesting directions for future research.Keywords
This publication has 131 references indexed in Scilit:
- Differential Ligand Binding Affinities of Human Estrogen Receptor-α IsoformsPLOS ONE, 2013
- Comprehensive molecular portraits of human breast tumoursNature, 2012
- Fatty Acid Synthase Modulates Intestinal Barrier Function through Palmitoylation of Mucin 2Cell Host & Microbe, 2012
- Tumor Metastasis: Molecular Insights and Evolving ParadigmsCell, 2011
- Cracking the Estrogen Receptor's Posttranslational Code in Breast TumorsEndocrine Reviews, 2011
- Mechanistic and signaling analysis of Muc4-ErbB2 signaling module: New insights into the mechanism of ligand-independent ErbB2 activityJournal of Cellular Physiology, 2010
- Genomic Antagonism between Retinoic Acid and Estrogen Signaling in Breast CancerCell, 2009
- Genes that mediate breast cancer metastasis to the brainNature, 2009
- Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylationNature, 2008
- Regulation of Estrogen Receptor α by the SET7 Lysine MethyltransferaseMolecular Cell, 2008