Enrichment of Cysteine S-palmitoylated Peptides Using Sodium Deoxycholate Acid Precipitation
Peter T. Jensen, Giuseppe Palmisano, Christopher J. Rhodes, Martin R. Larsen
TL;DR
The paper introduces a new method called SDC-ACE for efficiently identifying S-palmitoylated peptides, which helps study their role in cellular processes and diseases like diabetes.
Contribution
The novel SDC-ACE method enables fast and sensitive enrichment of S-palmitoylated peptides surpassing existing techniques.
Findings
More than 33,000 formerly S-palmitoylated peptides were identified from mouse brain.
SDC-ACE reveals tissue-specific S-palmitoylation events across mouse organs.
Regulated S-palmitoylated sites linked to obesity and diabetes were uncovered.
Abstract
S-palmitoylation is a poorly understood post-translational modification that is gaining more attention as an essential regulator of cellular processes. The reversible nature of S-palmitoylation may allow for fine-tuned control of cellular events and adaptation to stimuli. The detection of S-palmitoylated proteins and peptides includes the Acyl-Biotin Exchange (ABE) method, Acyl resin-assisted Capture (Acyl-RAC), metabolic labelling, and derivatives thereof. We present a novel method of enrichment of S-palmitoylated peptides termed SDC Acid Precipitation Enrichment (SDC-ACE). Here, S-palmitoylated peptides are enriched by taking advantage of their co-precipitation with Sodium deoxycholate (SDC) under acidic conditions, allowing easy and fast separation of lipidated peptides from the sample suspension. We initially applied our novel method for the characterization of the mouse brain,…
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Taxonomy
TopicsPeptidase Inhibition and Analysis · RNA modifications and cancer · Adenosine and Purinergic Signaling