ArticleCommunicative & integrative biology2018
Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin.
Article in Communicative & integrative biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation.The Journal of cell biology · 2026Article
- Naa80 is required for actin N-terminal acetylation and normal hearing in zebrafish.Life science alliance · 2024Article
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- An N-acetyltransferase required for EsxA N-terminal protein acetylation and virulence in Mycobacterium marinum.bioRxiv : the preprint server for biology · 2023Article
- Optimized bisubstrate inhibitors for the actin N-terminal acetyltransferase NAA80.Frontiers in chemistry · 2023Article
- The Final Maturation State of β-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1.Journal of molecular biology · 2022Article
- Myofilament glycation in diabetes reduces contractility by inhibiting tropomyosin movement, is rescued by cMyBPC domains.Journal of molecular and cellular cardiology · 2022Article
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- 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
- N-terminal acetylation of actin by NAA80 is essential for structural integrity of the Golgi apparatus.Experimental cell research · 2020Article
- Myosin and gelsolin cooperate in actin filament severing and actomyosin motor activity.The Journal of biological chemistryArticle
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.