ArticleExperimental cell research2020
N-terminal acetylation of actin by NAA80 is essential for structural integrity of the Golgi apparatus.
Article in Experimental cell research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation.The Journal of cell biology · 2026Article
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Naa80 is required for actin N-terminal acetylation and normal hearing in zebrafish.Life science alliance · 2024Article
- Biallelic NAA60 variants with impaired n-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications.Nature communications · 2024Article
- N-terminal acetyltransferase 6 facilitates enterovirus 71 replication by regulating PI4KB expression and replication organelle biogenesis.Journal of virology · 2024Article
- Optimized bisubstrate inhibitors for the actin N-terminal acetyltransferase NAA80.Frontiers in chemistry · 2023Article
- Identification of NAA40 as a Potential Prognostic Marker for Aggressive Liver Cancer Subtypes.Frontiers in oncology · 2021Article
- PFN2 and NAA80 cooperate to efficiently acetylate the N-terminus of actin.The Journal of biological chemistry · 2020Article
- Efficient and crucial quality control of HAP1 cell ploidy status.Biology open · 2020Article
- Exploiting the potential of commercial digital holographic microscopy by combining it with 3D matrix cell culture assays.Scientific reports · 2020Article
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Authors and funding
5 authors.
Funding
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Abstract
N-alpha-acetyltransferase 80 (NAA80) was recently demonstrated to acetylate the N-terminus of actin, with NAA80 knockout cells showing actin cytoskeleton-related phenotypes, such as increased formation of membrane protrusions and accelerated migration. Here we report that NAA80 knockout cells additionally display fragmentation of the Golgi apparatus. We further employed rescue assays to demonstrate that this phenotype is connected to the ability of NAA80 to modify actin. Thus, re-expression of NAA80, which leads to re-establishment of actin's N-terminal acetyl group, rescued the Golgi fragmentation, whereas a catalytic dead NAA80 mutant could neither restore actin Nt-acetylation nor Golgi structure. The Golgi phenotype of NAA80 KO cells was shared by both migrating and non-migrating cells and live-cell imaging indicated increased Golgi dynamics in migrating NAA80 KO cells. Finally, we detected a drastic increase in the amount of F-actin in cells lacking NAA80, suggesting a causal relationship between this effect and the observed re-organization of Golgi structure. The findings further underscore the importance of actin Nt-acetylation and provide novel insight into its cellular roles, suggesting a mechanistic link between actin modification state and Golgi organization.
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