Composition and biological significance of the human Nα-terminal acetyltransferases

被引：34
作者：
Kristian K Starheim
Darina Gromyko
Rolf Velde
Jan Erik Varhaug
Thomas Arnesen
机构：
[1] University of Bergen,Department of Molecular Biology
[2] University of Bergen,Department of Surgical Sciences
[3] Haukeland University Hospital,Department of Surgery
来源：
BMC Proceedings | / 3卷 / Suppl 6期
关键词：
Papillary Thyroid Carcinoma; Auxiliary Subunit; Thyroid Cell Line; Burkitt Lymphoma Cell Line; Knockdown Phenotype;
D O I：
10.1186/1753-6561-3-S6-S3
中图分类号：
学科分类号：
摘要：
Protein Nα-terminal acetylation is one of the most common protein modifications in eukaryotic cells, occurring on approximately 80% of soluble human proteins. An increasing number of studies links Nα-terminal acetylation to cell differentiation, cell cycle, cell survival, and cancer. Thus, Nα-terminal acetylation is an essential modification for normal cell function in humans. Still, little is known about the functional role of Nα-terminal acetylation. Recently, the three major human N-acetyltransferase complexes, hNatA, hNatB and hNatC, were identified and characterized. We here summarize the identified N-terminal acetyltransferase complexes in humans, and we review the biological studies on Nα-terminal acetylation in humans and other higher eukaryotes.
引用
收藏
相关论文
共 329 条
[1]  
Arnesen T(2005)Identification and characterization of the human ARD1-NATH protein acetyltransferase complex Biochem J 386 433-443
[2]  
Anderson D(2005)Interaction of N-terminal acetyltransferase with the cytoplasmic domain of beta-amyloid precursor protein and its effect on A beta secretion J Biochem (Tokyo) 137 147-155
[3]  
Baldersheim C(2008)Identification of the human N(alpha)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression Biochem J 415 325-331
[4]  
Lanotte M(2009)Knockdown of the Human N{alpha}-Terminal Acetyltransferase Complex C (hNatC) Leads to p53-Dependent Apoptosis and Aberrant hArl8b Localization Mol Cell Biol 29 3569-3581
[5]  
Varhaug JE(2006)Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex Gene 371 291-295
[6]  
Lillehaug JR(2007)The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner J Cell Biol 177 587-597
[7]  
Asaumi M(2003)N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins J Mol Biol 325 595-622
[8]  
Iijima K(2006)Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex Oncogene 25 4350-4360
[9]  
Sumioka A(2009)Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans Proc Natl Acad Sci USA 106 8157-8162
[10]  
Iijima-Ando K(2002)NATH, a novel gene overexpressed in papillary thyroid carcinomas Oncogene 21 5056-5068
12345678910