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Unravelling the role of lysine acetylation in the regulation of glycolysis in cancer cells through the development of synthetic biology-based tools

Total Cost €


EC-Contrib. €






Project "AcetyLys" data sheet

The following table provides information about the project.


Organization address
address: .
postcode: 84105

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Israel [IL]
 Project website
 Total cost 1˙499˙375 €
 EC max contribution 1˙499˙375 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2015-STG
 Funding Scheme ERC-STG
 Starting year 2016
 Duration (year-month-day) from 2016-07-01   to  2021-06-30


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    BEN-GURION UNIVERSITY OF THE NEGEV IL (BEER SHEVA) coordinator 1˙499˙375.00


 Project objective

Synthetic biology is an emerging discipline that offers powerful tools to control and manipulate fundamental processes in living matter. We propose to develop and apply such tools to modify the genetic code of cultured mammalian cells and bacteria with the aim to study the role of lysine acetylation in the regulation of metabolism and in cancer development. Thousands of lysine acetylation sites were recently discovered on non-histone proteins, suggesting that acetylation is a widespread and evolutionarily conserved post translational modification, similar in scope to phosphorylation and ubiquitination. Specifically, it has been found that most of the enzymes of metabolic processes—including glycolysis—are acetylated, implying that acetylation is key regulator of cellular metabolism in general and in glycolysis in particular. The regulation of metabolic pathways is of particular importance to cancer research, as misregulation of metabolic pathways, especially upregulation of glycolysis, is common to most transformed cells and is now considered a new hallmark of cancer. These data raise an immediate question: what is the role of acetylation in the regulation of glycolysis and in the metabolic reprogramming of cancer cells? While current methods rely on mutational analyses, we will genetically encode the incorporation of acetylated lysine and directly measure the functional role of each acetylation site in cancerous and non-cancerous cell lines. Using this methodology, we will study the structural and functional implications of all the acetylation sites in glycolytic enzymes. We will also decipher the mechanism by which acetylation is regulated by deacetylases and answer a long standing question – how 18 deacetylases recognise their substrates among thousands of acetylated proteins? The developed methodologies can be applied to a wide range of protein families known to be acetylated, thereby making this study relevant to diverse research fields.


year authors and title journal last update
List of publications.
2019 Sarit Cohen, Lior Kramarski, Shahar Levi, Noa Deshe, Oshrit Ben David, Eyal Arbely
Nonsense mutation-dependent reinitiation of translation in mammalian cells
published pages: , ISSN: 0305-1048, DOI: 10.1093/nar/gkz319
Nucleic Acids Research 2019-09-02
2018 Emanuel M. Avrahami, Shahar Levi, Eyal Zajfman, Clil Regev, Oshrit Ben-David, Eyal Arbely
Reconstitution of Mammalian Enzymatic Deacylation Reactions in Live Bacteria Using Native Acylated Substrates
published pages: 2348-2354, ISSN: 2161-5063, DOI: 10.1021/acssynbio.8b00314
ACS Synthetic Biology 7/10 2019-03-11
2018 Noa Aloush, Tomer Schvartz, Andres I. König, Sarit Cohen, Eugene Brozgol, Benjamin Tam, Dikla Nachmias, Oshrit Ben-David, Yuval Garini, Natalie Elia, Eyal Arbely
Live Cell Imaging of Bioorthogonally Labelled Proteins Generated With a Single Pyrrolysine tRNA Gene
published pages: , ISSN: 2045-2322, DOI: 10.1038/s41598-018-32824-1
Scientific Reports 8/1 2019-03-11
2018 Michael Muzika, Natali H. Muskat, Shani Sarid, Oshrit Ben-David, Ryan A. Mehl, Eyal Arbely
Chemically-defined lactose-based autoinduction medium for site-specific incorporation of non-canonical amino acids into proteins
published pages: 25558-25567, ISSN: 2046-2069, DOI: 10.1039/c8ra04359k
RSC Advances 8/45 2019-03-11

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