Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.

Edmonds, MJ, Geary, B, Doherty, MK and Morgan, A ORCID: 0000-0002-0346-1289 (2017) Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods. Scientific reports, 7 (1).

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Official URL: http://dx.doi.org/10.1038/s41598-017-03562-7

Abstract

Palmitoylation is a reversible post-translational protein modification in which palmitic acid is added to cysteine residues, allowing association with different cellular membranes and subdomains. Recently, techniques have been developed to identify palmitoylation on a proteome-wide scale in order to reveal the full cellular complement of palmitoylated proteins. However, in the studies reported to date, there is considerable variation between the sets of identified palmitoyl-proteins and so there remains some uncertainty over what constitutes the definitive complement of palmitoylated proteins even in well-studied tissues such as brain. To address this issue, we used both acyl-biotin exchange and acyl-resin-assisted capture approaches using rat brain as a common protein source. The palmitoyl-proteins identified from each method by mass spectrometry were then compared with each other and previously published studies. There was generally good agreement between the two methods, although many identifications were unique to one method, indicating that at least some of the variability in published palmitoyl proteomes is due to methodological differences. By combining our new data with previous publications using mammalian cells/tissues, we propose a high confidence set of bona fide palmitoylated proteins in brain and provide a resource to help researchers prioritise candidate palmitoyl-proteins for investigation.

Item Type:	Article
Uncontrolled Keywords:	Brain, Animals, Rats, Biotin, Resins, Synthetic, Palmitic Acid, Proteome, Proteomics, Acylation, Mass Spectrometry, Lipoylation
Depositing User:	Symplectic Admin
Date Deposited:	22 Jun 2017 11:40
Last Modified:	19 Jan 2023 07:02
DOI:	10.1038/s41598-017-03562-7
Open Access URL:	https://www.nature.com/articles/s41598-017-03562-7
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3008107