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Arnesen lab

The eukaryotic NAT-machinery

Protein N-terminal acetylation

From molecular mechanisms to human disease

Most proteins are chemically modified in the cell and such modifications are often crucial for the protein’s ability to carry out a function. N-terminal acetylation one of the most common modifications in eukaryotes. It is catalyzed by N-terminal acetyltransferases (NATs) which are linked to cancer, genetic syndromes, and regulation of human metabolism.

The Arnesen lab is part of the Translational Cell Signaling and Metabolism research group at the Department of biomedicine.

New research
Structure of actin, profilin and NAA80

Mechanism of a cell motility regulator

Actin is the most abundant protein in human cells and is involved in numerous functions including steering cellular architecture, cell motility and cell division. Recently, UiB researchers identified NAA80 as a long-sought actin regulator. Now, the structure of NAA80 bound to actin and profilin...

Cell biology
Cryo-EM structures of the NatE complex with/without HYPK bound

The structure of an enzyme complex upregulated in cancer

In human cells, N-terminal acetylation is among the most common protein modifications. Now, researchers at the University of Pennsylvania and the University of Bergen have revealed the structural and biochemical properties of the major molecular machine involved in this process. Cancer cells require...

Faculty Day 2020
Marte Bjørk, Henriette Aksnes og Nils Erik Gilhus

Faculty Day 2020 - Award Winners

Here are the award winners of Faculty Day 2020!

Award
To forskningsartikkler stemplet med Best paper 2018

Paper of the year 2018

Two PNAS articles from the Arnesen lab are elected as the best publication of the year 2018 at the Faculty of Medicine. The prize will be awarded at the Faculty Day on 13 June 2019.

New research
Hunger is not a hindrance for N-terminal acetylation

Hunger is not a hindrance for N-terminal acetylation

Arnesen Lab reveals that the global level of N-terminal acetylation, a highly abundant protein modification in eukaryotes, remains stable in starving yeast cells despite an overall decrease in the cellular level of acetyl-CoA. The findings, described in the December issue of Molecular & Cellular...