Related Experiment Video
Updated: Feb 1, 2026

In Vitro Polymerization of F-actin on Early Endosomes
Published on: August 28, 2017
Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of
Henriette Aksnes1, Michael Marie1, Thomas Arnesen1,2,3
1Department of Biomedicine, University of Bergen, Bergen, Norway.
Abstract:
Actin is the most abundant protein in our cells, and also one of the most studied. Nevertheless, an important modifier of actin, the N-terminal acetyltransferase (NAT) for actin, remained unknown until now. The recent identification of the enzyme that catalyzes actin acetylation, has opened up for functional studies of unacetylated actin using knockout cells. This enzyme, called NAA80 (Nα-acetyltransferase 80) or NatH, belongs to the NAT family of enzymes, which together provides N-terminal acetylation for around 80 % of the human proteome. In many cases, N-terminal acetylation is essential. In the case of actin, the acetyl group that NAA80 attaches to actin plays an important role in actin's polymerization properties as well as in actin's function in cell migration.
Related Concept Videos
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
Actin Polymerization
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
Actin Treadmilling
The Role of Actin and Myosin in Non-muscle Cells
Introduction to Actin
Actin Filament Depolymerization
In F-actin, the ADF/cofilin proteins...

