Doerfel, Max, Lyon, Gholson J. (August 2015) The biological functions of Naa10 – from amino-terminal acetylation to human disease. Gene, 567 (2). pp. 103-131. ISSN 0378-1119
Abstract
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.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | amino-terminal acetylation acetyltransferases proteins proteomics enzymology Ogden Syndrome NAA10 NAA15 NAA50 ard1 |
| Subjects: | diseases & disorders > congenital hereditary genetic diseases diseases & disorders bioinformatics > genomics and proteomics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > N-terminal acetylation |
| CSHL Authors: | |
| Communities: | CSHL labs > Lyon lab Stanley Institute for Cognitive Genomics |
| Depositing User: | Matt Covey |
| Date: | 10 August 2015 |
| Date Deposited: | 19 May 2015 19:53 |
| Last Modified: | 30 Jan 2017 15:51 |
| PMCID: | PMC4461483 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/31502 |
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