Abstract

Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl-proteomes of a variety of cell lines and tissues from different species. As the amount of information generated by these high-throughput studies is increasing, the field requires centralization and comparison of this information. Here we present SwissPalm ( http://swisspalm.epfl.ch), our open, comprehensive, manually curated resource to study protein S-palmitoylation. It currently encompasses more than 5000 S-palmitoylated protein hits from seven species, and contains more than 500 specific sites of S-palmitoylation. SwissPalm also provides curated information and filters that increase the confidence in true positive hits, and integrates predictions of S-palmitoylated cysteine scores, orthologs and isoform multiple alignments. Systems analysis of the palmitoyl-proteome screens indicate that 10% or more of the human proteome is susceptible to S-palmitoylation. Moreover, ontology and pathway analyses of the human palmitoyl-proteome reveal that key biological functions involve this reversible lipid modification. Comparative analysis finally shows a strong crosstalk between S-palmitoylation and other post-translational modifications. Through the compilation of data and continuous updates, SwissPalm will provide a powerful tool to unravel the global importance of protein S-palmitoylation.

Highlights

  • S-palmitoylation is defined as the enzymatic attachment of a 16carbon-chain palmitic acid to cysteine residues via a thioester bond[1,2]

  • Palmitoyl-proteomes. 19 palmitoyl-proteome screens using Acyl Biotin Exchange (ABE), Acyl-RAC- or click chemistry-based studies were selected from published literature

  • They cover seven species and ten palmitoyl proteomes performed with ABE, 2 with Acyl-RAC and 7 with click chemistry (Figure 1A)

Read more

Summary

Introduction

S-palmitoylation is defined as the enzymatic attachment of a 16carbon-chain palmitic acid to cysteine residues via a thioester bond[1,2]. S-palmitoylation appears to occur in all eukaryotes since it was found in yeast, parasites, worm, flies and plants. It is the only reversible lipid post-translational modification (PTM) identified to date[13] and can dynamically regulate the function of proteins. The dynamics of S-palmitoylation are mediated by the opposing activities of two families of enzymes: palmitoyltransferases (PATs), which catalyze the attachment of palmitate to specific cysteine residues while thioesterases detach it[5,16,17] and Acyl Protein Thioesterases (APTS) which remove the acyl chain

Methods
Results
Conclusion
Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.