Expression of human<i>NAA11</i>(<i>ARD1B</i>) gene is tissue-specific and is regulated by DNA methylation

Pang, Alan Lap‐Yin; Clark, Jason D.; Chan, Wai‐Yee; Rennert, Owen M.

doi:10.4161/epi.6.11.18125

Cited by 19 publications

(20 citation statements)

References 37 publications

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“…Additionally, a processed NAA10 gene duplicate NAA11 (ARD2) has been identified that is expressed in several human cell lines including Jurkat, HEK293 and NPA (Arnesen et al, 2006b). However, later studies have revealed data arguing that Naa11 is not expressed in the human cell lines HeLa and HEK293 or in cancerous tissues, and NAA11 transcripts were only detected in testicular and placental tissues (Pang et al, 2011). Therefore, the functional role of Naa11 might be constricted to certain tissues only.…”

Section: Introductionmentioning

confidence: 99%

The biological functions of Naa10 — From amino-terminal acetylation to human disease

Dörfel

Lyon

2015

Gene

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N-terminal acetylation (NTA) is one of the most abundant protein modifications known, and the N-terminal acetyltransferase (NAT) machinery is conserved throughout all Eukarya. Over the past 50 years, the function of NTA has begun to be slowly elucidated, and this includes the modulation of protein–protein interaction, protein-stability, protein function, and protein targeting to specific cellular compartments. Many of these functions have been studied in the context of Naa10/NatA; however, we are only starting to really understand the full complexity of this picture. Roughly, about 40% of all human proteins are substrates of Naa10 and the impact of this modification has only been studied for a few of them. Besides acting as a NAT in the NatA complex, recently other functions have been linked to Naa10, including post-translational NTA, lysine acetylation, and NAT/KAT-independent functions. Also, recent publications have linked mutations in Naa10 to various diseases, emphasizing the importance of Naa10 research in humans. The recent design and synthesis of the first bisubstrate inhibitors that potently and selectively inhibit the NatA/Naa10 complex, monomeric Naa10, and hNaa50 further increases the toolset to analyze Naa10 function.

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Section: Introductionmentioning

confidence: 99%

The biological functions of Naa10 — From amino-terminal acetylation to human disease

Dörfel

Lyon

2015

Gene

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“…While most acetylation studies have focused on chromatin-associated proteins, acetylation of non-chromatin proteins has been less thoroughly explored. There are multiple genes that encode acetyltransferases [ 18 – 20 ], including ARD1 of which there are two isoforms: ARD1A and ARD1B [ 21 ]. It is believed that ARD1B is a bona fide retrogene of ARD1A [ 22 ].…”

Section: Introductionmentioning

confidence: 99%

Acetylation and deacetylation of Cdc25A constitutes a novel mechanism for modulating Cdc25A functions with implications for cancer

et al. 2016

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The dual specificity phosphatase Cdc25A is a key regulator of the cell cycle that promotes cell cycle progression by dephosphorylating and activating cyclin-dependent kinases. In response to genotoxicants, Cdc25A undergoes posttranslational modifications which contribute to its proteasome-mediated degradation and consequent cell cycle checkpoint arrest. The most thoroughly studied Cdc25A modification is phosphorylation. We now provide the first evidence that Cdc25A can be acetylated and that it directly interacts with the ARD1 acetyltransferase which acetylates Cdc25A both biochemically and in cultured cells. When acetylated, Cdc25A has an extended half-life. We have also identified the class IV histone deacetylase, HDAC11, as a Cdc25A deacetylase. We further show that DNA damage, such as exposure to methyl methanesulfonate (MMS), etoposide or arsenic, increases Cdc25A acetylation. Importantly, this acetylation modulates Cdc25A phosphatase activity and its function as a cell cycle regulator, and may reflect a cellular response to DNA damage. Since Cdc25A, ARD1, and HDAC11 are frequently dysregulated in multiple types of cancer, our findings may provide insight into a novel mechanism in carcinogenesis.

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“…NAA11 (also known as Ard1b; ARD2 ), a homolog of NAA10 , is predominantly expressed in mouse 57 and human 58 testis. Naa11 can reconstitute functional NAT in the presence of Naa15, where Naa11 is functionally equivalent to Naa10.…”

Section: N-terminal Acetylation Dependent Functions Of Naa10 During Ementioning

confidence: 99%

N-α-acetyltransferase 10 (NAA10) in development: the role of NAA10

Lee

Kweon

2018

Exp Mol Med

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N-α-acetyltransferase 10 (NAA10) is a subunit of Nα-terminal protein acetyltransferase that plays a role in many biological processes. Among the six N-α-acetyltransferases (NATs) in eukaryotes, the biological significance of the N-terminal acetyl-activity of Naa10 has been the most studied. Recent findings in a few species, including humans, indicate that loss of N-terminal acetylation by NAA10 is associated with developmental defects. However, very little is known about the role of NAA10, and more research is required in relation to the developmental process. This review summarizes recent studies to understand the function of NAA10 in the development of multicellular organisms.

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Expression of humanNAA11(ARD1B) gene is tissue-specific and is regulated by DNA methylation

Cited by 19 publications

References 37 publications

The biological functions of Naa10 — From amino-terminal acetylation to human disease

The biological functions of Naa10 — From amino-terminal acetylation to human disease

Acetylation and deacetylation of Cdc25A constitutes a novel mechanism for modulating Cdc25A functions with implications for cancer

N-α-acetyltransferase 10 (NAA10) in development: the role of NAA10

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