Correlation of Expression of Human Arrest-Defective-1 (hARD1) Protein With Breast Cancer

Yu, Min; Ma, Mingxing; Huang, Chao; Yang, Hui; Lai, Jianhua; Yan, Shanchun; Lin, Li; Xiang, Mingjun; Tan, Dezhi

doi:10.3109/07357900902769723

Cited by 33 publications

(23 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Overexpression of Naa10 increased cell proliferation in breast cancer cells by promoting the cells to pass the G1/S and G2/M cell cycle checkpoints [141]. HeLa cells depleted for NatA showed a reduced viability due to activation of a p53-dependent apoptosis [143], a phenotype also found in colon carcinoma reporting a p53-independent growth inhibition [144].…”

Section: Naa10 and Naa15 Function As Oncogenesmentioning

confidence: 98%

“…Different cancer types and tissue display elevated levels of Naa10 expression including hepatocellular carcinoma [131], colorectal cancer [138,139], lung cancer [139,140], breast cancer [139,141] and prostate cancer [142]. Overexpression of Naa10 was also reported in urinary bladder cancer, breast cancer and cervical carcinoma [139].…”

Section: Naa10 and Naa15 Function As Oncogenesmentioning

confidence: 99%

See 1 more Smart Citation

The world of protein acetylation

Drazic

Myklebust

Ree

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

646

532

View full text Add to dashboard Cite

Acetylation is one of the major post-translational protein modifications in the cell, with manifold effects on the protein level as well as on the metabolome level. The acetyl group, donated by the metabolite acetyl-coenzyme A, can be co- or post-translationally attached to either the α-amino group of the N-terminus of proteins or to the ε-amino group of lysine residues. These reactions are catalyzed by various N-terminal and lysine acetyltransferases. In case of lysine acetylation, the reaction is enzymatically reversible via tightly regulated and metabolism-dependent mechanisms. The interplay between acetylation and deacetylation is crucial for many important cellular processes. In recent years, our understanding of protein acetylation has increased significantly by global proteomics analyses and in depth functional studies. This review gives a general overview of protein acetylation and the respective acetyltransferases, and focuses on the regulation of metabolic processes and physiological consequences that come along with protein acetylation.

show abstract

Section: Naa10 and Naa15 Function As Oncogenesmentioning

confidence: 98%

Section: Naa10 and Naa15 Function As Oncogenesmentioning

confidence: 99%

The world of protein acetylation

Drazic

Myklebust

Ree

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

646

532

View full text Add to dashboard Cite

show abstract

“…Further studies have shown that ARD1 is present in various species, including the mouse, rat, chimpanzee, and human, and has several variants, playing different roles [3]–[6]. In humans, human ARD1 235 (hARD1) is the major form, involved in diverse biological processes, such as cell proliferation, differentiation, autophagy, and cancer [7]–[13].…”

Section: Introductionmentioning

confidence: 99%

Nuclear Translocation of hARD1 Contributes to Proper Cell Cycle Progression

et al. 2014

View full text Add to dashboard Cite

Arrest defective 1 (ARD1) is an acetyltransferase that is highly conserved across organisms, from yeasts to humans. The high homology and widespread expression of ARD1 across multiple species and tissues signify that it serves a fundamental role in cells. Human ARD1 (hARD1) has been suggested to be involved in diverse biological processes, and its role in cell proliferation and cancer development has been recently drawing attention. However, the subcellular localization of ARD1 and its relevance to cellular function remain largely unknown. Here, we have demonstrated that hARD1 is imported to the nuclei of proliferating cells, especially during S phase. Nuclear localization signal (NLS)-deleted hARD1 (hARD1ΔN), which can no longer access the nucleus, resulted in cell morphology changes and cellular growth impairment. Notably, hARD1ΔN-expressing cells showed alterations in the cell cycle and the expression levels of cell cycle regulators compared to hARD1 wild-type cells. Furthermore, these effects were rescued when the nuclear import of hARD1 was restored by exogenous NLS. Our results show that hARD1 nuclear translocation mediated by NLS is required for cell cycle progression, thereby contributing to proper cell proliferation.

show abstract

“…□ S The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1 cancer cell lines, and NatA knockdown results in a decrease in cellular proliferation and induction of apoptosis (15)(16)(17)(18). NATs have therefore become an attractive chemotherapeutic target, further driving the need for a molecular understanding of how these enzymes carry out their functions.…”

mentioning

confidence: 99%

Structure of a Ternary Naa50p (NAT5/SAN) N-terminal Acetyltransferase Complex Reveals the Molecular Basis for Substrate-specific Acetylation

Liszczak

Arnesen

Marmorstein

2011

Journal of Biological Chemistry

165

View full text Add to dashboard Cite

Background:The human Naa50p N-terminal acetyltransferase acetylates proteins on the ␣-amino group of methionine residues to regulate genome integrity and has elevated activity in cancer. Results: We report the structure of the Naa50p⅐CoA⅐peptide complex and related biochemistry. Conclusion: We reveal the molecular basis for substrate-specific acetylation by Naa50p. Significance: We provide a molecular scaffold for the design of Naa50p-specific inhibitors with possible therapeutic applications.

show abstract

Correlation of Expression of Human Arrest-Defective-1 (hARD1) Protein With Breast Cancer

Cited by 33 publications

References 22 publications

The world of protein acetylation

The world of protein acetylation

Nuclear Translocation of hARD1 Contributes to Proper Cell Cycle Progression

Structure of a Ternary Naa50p (NAT5/SAN) N-terminal Acetyltransferase Complex Reveals the Molecular Basis for Substrate-specific Acetylation

Contact Info

Product

Resources

About