System-Wide Analysis of Protein Acetylation and Ubiquitination Reveals a Diversified Regulation in Human Cancer Cells.

Biomolecules
Hiroko Kozuka-HataMasaaki Oyama

Abstract

Post-translational modifications are known to be widely involved in the regulation of various biological processes, through the extensive diversification of each protein function at the cellular network level. In order to unveil the system-wide function of the protein lysine modification in cancer cell signaling, we performed global acetylation and ubiquitination proteome analyses of human cancer cells, based on high-resolution nanoflow liquid chromatography-tandem mass spectrometry, in combination with the efficient biochemical enrichment of target modified peptides. Our large-scale proteomic analysis enabled us to identify more than 5000 kinds of ubiquitinated sites and 1600 kinds of acetylated sites, from representative human cancer cell lines, leading to the identification of approximately 900 novel lysine modification sites in total. Very interestingly, 236 lysine residues derived from 141 proteins were found to be modified with both ubiquitination and acetylation. As a consequence of the subsequent motif extraction analyses, glutamic acid (E) was found to be highly enriched at the position (-1) for the lysine acetylation sites, whereas the same amino acid was relatively dispersed along the neighboring residues of the lysi...Continue Reading

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Methods Mentioned

BETA
acetylation
ubiquitination
Protein
dissection

Software Mentioned

PhosphoSitePlus
motif
Mascot
Ingenuity Pathway Analysis ( IPA
Unimod
IPA
Ingenuity Knowledge Base

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