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- W2006897037 abstract "The human N-terminal acetyltransferases (NATs) catalyze the transfer of acetyl moieties to the N-termini of 80–90% of all human proteins. Six NAT types are present in humans, NatA–NatF, each is composed of specific subunits and each acetylates a set of substrates defined by the N-terminal amino-acid sequence. NATs have been suggested to act as oncoproteins as well as tumor suppressors in human cancers, and NAT expression may be both elevated and decreased in cancer versus non-cancer tissues. Manipulation of NATs in cancer cells induced cell-cycle arrest, apoptosis or autophagy, implying that these enzymes target a variety of pathways. Of particular interest is hNaa10p (human ARD1), the catalytic subunit of the NatA complex, which was coupled to a number of signaling molecules including hypoxia inducible factor-1α, β-catenin/cyclin D1, TSC2/mammalian target of rapamycin, myosin light chain kinase , DNA methyltransferase1/E-cadherin and p21-activated kinase-interacting exchange factors (PIX)/Cdc42/Rac1. The variety of mechanistic links where hNaa10p acts as a NAT, a lysine acetyltransferase or displaying a non-catalytic role, provide insights to how hNaa10p may act as both a tumor suppressor and oncoprotein." @default.
- W2006897037 created "2016-06-24" @default.
- W2006897037 creator A5032682346 @default.
- W2006897037 creator A5043906785 @default.
- W2006897037 date "2012-03-05" @default.
- W2006897037 modified "2023-10-16" @default.
- W2006897037 title "Protein N-terminal acetyltransferases in cancer" @default.
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- W2006897037 doi "https://doi.org/10.1038/onc.2012.82" @default.
- W2006897037 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22391571" @default.
- W2006897037 hasPublicationYear "2012" @default.
- W2006897037 type Work @default.