ArticleThe Biochemical journal2005
Identification and characterization of the human ARD1-NATH protein acetyltransferase complex.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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Who cites it
112 citing papers in PubMed, 205 citations in OpenAlex.
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- The Cardiovascular Manifestations and Management Recommendations for Ogden Syndrome.Pediatric cardiology · 2026Article
- LRRC75A-AS1 facilitates breast cancer cell proliferation and invasion via functioning as a CeRNA to modulate miR489-3p/ARD1.Scientific reports · 2025Article
- NAA10 (N-Alpha-Acetyltransferase 10): A Multifunctional Regulator in Development, Disease, and Cancer.Cells · 2025Review
- Natural History of NAA15 -Related Neurodevelopmental Disorder Through Adolescence.American journal of medical genetics. Part A · 2025Article
- Dysregulation of N-terminal acetylation causes cardiac arrhythmia and cardiomyopathy.Nature communications · 2025Article
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Conformational plasticity links structural instability of NAA10Computational and structural biotechnology journal · 2024Article
- A repository of Ogden syndrome patient derived iPSC lines and isogenic pairs by X-chromosome screening and genome-editing.bioRxiv : the preprint server for biology · 2024Article
- N-terminal cysteine acetylation and oxidation patterns may define protein stability.Nature communications · 2024Article
- Evaluating possible maternal effect lethality and genetic background effects inbioRxiv : the preprint server for biology · 2024Article
- Evaluating possible maternal effect lethality and genetic background effects in Naa10 knockout mice.PloS one · 2024Article
- Article
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- Expanding the phenotypic spectrum of NAA10-related neurodevelopmental syndrome and NAA15-related neurodevelopmental syndrome.European journal of human genetics : EJHG · 2023Article
- Clinical manifestations in a Chinese girl with heterozygousFrontiers in pediatrics · 2023Article
- A Case ofCJC pediatric and congenital heart disease · 2022Article
- Naa10p promotes cell invasiveness of esophageal cancer by coordinating the c-Myc and PAI1 regulatory axis.Cell death & disease · 2022Article
- From Nucleus to Membrane: A Subcellular Map of the N-Acetylation Machinery in Plants.International journal of molecular sciences · 2022Review
52 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein acetyltransferases and deacetylases have been implicated in oncogenesis, apoptosis and cell cycle regulation. Most of the protein acetyltransferases described acetylate epsilon-amino groups of lysine residues within proteins. Mouse ARD1 (homologue of yeast Ard1p, where Ard1p stands for arrest defective 1 protein) is the only known protein acetyltransferase catalysing acetylation of proteins at both alpha-(N-terminus) and epsilon-amino groups. Yeast Ard1p interacts with Nat1p (N-acetyltransferase 1 protein) to form a functional NAT (N-acetyltransferase). We now describe the human homologue of Nat1p, NATH (NAT human), as the partner of the hARD1 (human ARD1) protein. Included in the characterization of the NATH and hARD1 proteins is the following: (i) endogenous NATH and hARD1 proteins are expressed in human epithelial, glioma and promyelocytic cell lines; (ii) NATH and hARD1 form a stable complex, as investigated by reciprocal immunoprecipitations followed by MS analysis; (iii) NATH-hARD1 complex expresses N-terminal acetylation activity; (iv) NATH and hARD1 interact with ribosomal subunits, indicating a co-translational acetyltransferase function; (v) NATH is localized in the cytoplasm, whereas hARD1 localizes both to the cytoplasm and nucleus; (vi) hARD1 partially co-localizes in nuclear spots with the transcription factor HIF-1alpha (hypoxia-inducible factor 1alpha), a known epsilon-amino substrate of ARD1; (vii) NATH and hARD1 are cleaved during apoptosis, resulting in a decreased NAT activity. This study identifies the human homologues of the yeast Ard1p and Nat1p proteins and presents new aspects of the NATH and hARD1 proteins relative to their yeast homologues.
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