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Discovery and functional significance of post-translational N-terminal acetylation

Total Cost €


EC-Contrib. €






Project "NterAct" data sheet

The following table provides information about the project.


Organization address
address: MUSEPLASSEN 1
city: BERGEN
postcode: 5020

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 Norway [NO]
 Project website
 Total cost 1˙999˙273 €
 EC max contribution 1˙999˙273 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2017-COG
 Funding Scheme ERC-COG
 Starting year 2018
 Duration (year-month-day) from 2018-06-01   to  2023-05-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITETET I BERGEN NO (BERGEN) coordinator 1˙999˙273.00


 Project objective

In mammalian cells, N-terminal (Nt) acetylation is one of the most abundant protein modifications. It is catalysed by N-terminal acetyltransferases (NATs) and mostly occurs co-translationally. However, in contrast to the defined co-translational NATs, post-translational NATs which have crucial regulatory roles are mostly unexplored. Distinct peptide hormones regulate appetite, metabolism, sexual behaviour and pain, and their biological activity is critically modulated by post-translational Nt-acetylation. However, the identity of the NAT responsible for this modification, ‘HormNat’, is unknown, thus the molecular and physiological ramifications of this regulatory circuit remain elusive. Another example is actin, a key regulator of cell motility and cell division. The actin N-terminus is crucial for actin function and in mammals actin is modified by an unknown post-translational NAT, ‘ActNat’. Hence, the objectives of this project are to identify these human NATs acting post-translationally, and to investigate their molecular mechanisms, regulation and impact.

We will identify the novel NATs by a combination of classical and newly developed in-house tools like in vitro acetylation assays, unique bisubstrate analogues, Nt-acetylation specific antibodies, and targeted mass spectrometry. Interestingly, Nt-acetylation is considered irreversible, but there is reason to believe that specific substrates are Nt-deacetylated. Elucidation of post-translational NATs and the reversible nature of Nt-acetylation would represent a new era in the field of protein and peptide regulation and identify key cellular and organismal switches.


year authors and title journal last update
List of publications.
2019 Henriette Aksnes, Rasmus Ree, Thomas Arnesen
Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases
published pages: 1097-1114, ISSN: 1097-2765, DOI: 10.1016/j.molcel.2019.02.007
Molecular Cell 73/6 2020-01-30
2018 Henriette Aksnes, Michael Marie, Thomas Arnesen, Adrian Drazic
Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin
published pages: e1526572, ISSN: 1942-0889, DOI: 10.1080/19420889.2018.1526572
Communicative & Integrative Biology 11/4 2020-01-30

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