Sun L et al. (2018), Comparative Phospho- and Acetyl Proteomics Anal...

ECB-ART-46476

Front Physiol January 1, 2018; 9 836.

Comparative Phospho- and Acetyl Proteomics Analysis of Posttranslational Modifications Regulating Intestine Regeneration in Sea Cucumbers.

Sun L , Lin C , Li X , Xing L , Huo D , Sun J , Zhang L , Yang H .

Abstract
Sea cucumbers exposed to stressful circumstances eviscerate most internal organs, and then regenerate them rapidly under favorable environments. Reversible protein phosphorylation and acetylation are major modifications regulating protein function. Herein, for the first time, we perform quantitative phospho- and acetyl proteomics analyses of intestine regeneration in a sea cucumber species Apostichopus japonicus. We identified 1,862 phosphorylation sites in 1,169 proteins, and 712 acetylation sites in 470 proteins. Of the 147 and 251 proteins differentially modified by phosphorylation and acetylation, respectively, most were related to cytoskeleton biogenesis, protein synthesis and modification, signal recognition and transduction, energy production and conversion, or substance transport and metabolism. Phosphorylation appears to play a more important role in signal recognition and transduction than acetylation, while acetylation is of greater importance in posttranslational modification, protein turnover, chaperones; energy production and conversion; amino acid and lipid transport and metabolism. These results expanded our understanding of the regulatory mechanisms of posttranslational modifications in intestine regeneration of sea cucumbers after evisceration.

PubMed ID: 30018572
PMC ID: PMC6037860
Article link: Front Physiol

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References [+] :

Arnold RJ, The action of N-terminal acetyltransferases on yeast ribosomal proteins. 1999, Pubmed

	Figure 1. Outline of the experiment design for phosphorylation and acetylation modification study. Control, the normal intestine in the sea cucumber. 3 dpe, the regenerative intestine at 3 days post evisceration.
	Figure 2. Enriched gene ontology (GO) analysis of differentially phosphorylated and acetylated proteins (p <0.05). (A) phosphorylation. (B) Acetylation. Red, GO terms of proteins for which the modification was upregulated. Green, GO terms of proteins for which the modification was downregulated.
	Figure 3. Protein domain enrichment analysis of differentially phosphorylated and acetylated proteins (p <0.05). (A) phosphorylation. (B) Acetylation. Red, Protein domain terms for which the modification was upregulated. Green, Protein domain terms for which the modification was downregulated.
	Figure 4. Enriched pathways analysis of differentially phosphorylated and acetylated proteins (all p <0.05). (A) phosphorylation. (B) Acetylation. Red, Pathways terms of proteins for which the modification was upregulated. Green, Pathways terms of proteins for which the modification was downregulated.
	Figure 5. Subcellular location of differentially phosphorylated and acetylated proteins. (A) phosphorylation. (B) acetylation. Up, subcellular location of proteins for which the modification was upregulated. Down, subcellular location of proteins for which the modification was downregulated.
	Figure 6. Schematic model of phosphorylation and acetylation during intestine regeneration in sea cucumbers. +, modification levels of almost all proteins were upregulated; −, modification levels of almost all proteins were downregulated; ±, modification levels of proteins were up- or downregulated. P, phosphorylation; Ac, acetylation; Big P or Ac, a large number of proteins were regulated by this reversible modification.
	Figure 7. Western blotting of pan-acetylation during intestine regeneration in sea cucumbers. Cell lysate samples contain 20 μg of total protein per lane. Proteins with a molecular weight of ~10 kb are likely histone family member.