Role of the staphylococcal nuclease and tudor domain containing 1 in oncogenesis (Review)

Arginine methylation is an essential post-translational modification (PTM) deposited by protein arginine methyltransferases (PRMTs) and recognized by Tudor domain-containing proteins. Of the nine mammalian PRMTs, PRMT5 is the primary enzyme responsible for the deposition of symmetric arginine methylation marks in cells. The staphylococcal nuclease and Tudor domain-containing 1 (SND1) effector protein is a key reader of the marks deposited by PRMT5. Both PRMT5 and SND1 are broadly expressed and their deregulation is reported to be associated with a range of disease phenotypes, including cancer. Hepatocellular carcinoma (HCC) is an example of a cancer type that often displays elevated PRMT5 and SND1 levels, and there is evidence that hyperactivation of this axis is oncogenic. Importantly, this pathway can be tempered with small-molecule inhibitors that target PRMT5, offering a therapeutic node for cancer, such as HCC, that display high PRMT5–SND1 axis activity. Here we summarize the known activities of this writer–reader pair, with a focus on their biological roles in HCC. This will help establish a foundation for treating HCC with PRMT5 inhibitors and also identify potential biomarkers that could predict sensitivity to this type of therapy.

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Local stability identification and the role of a key aromatic amino acid residue in staphylococcal nuclease refolding

FEBS Journal ◽

10.1111/j.1742-4658.2005.04814.x ◽

2005 ◽

Vol 272 (15) ◽

pp. 3960-3966 ◽

Cited By ~ 5

Author(s):

Zhengding Su ◽

Jiun-Ming Wu ◽

Huey-Jen Fang ◽

Tian-Yow Tsong ◽

Hueih-Min Chen

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Aromatic Amino Acid ◽

Local Stability ◽

Staphylococcal Nuclease ◽

Aromatic Amino Acid Residue

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Posttranscriptional Inhibition of Protein Tyrosine Phosphatase Nonreceptor Type 23 by Staphylococcal Nuclease and Tudor Domain Containing 1: Implications for Hepatocellular Carcinoma

Hepatology Communications ◽

10.1002/hep4.1400 ◽

2019 ◽

Vol 3 (9) ◽

pp. 1258-1270 ◽

Cited By ~ 3

Author(s):

Nidhi Jariwala ◽

Rachel G. Mendoza ◽

Dawn Garcia ◽

Zhao Lai ◽

Mark A. Subler ◽

...

Keyword(s):

Hepatocellular Carcinoma ◽

Protein Tyrosine Phosphatase ◽

Tyrosine Phosphatase ◽

Staphylococcal Nuclease ◽

Protein Tyrosine ◽

Tudor Domain

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1P-013 The role of the flexible loop in staphylococcal nuclease on its catalytic activity(The 46th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri ◽

10.2142/biophys.48.s22_6 ◽

2008 ◽

Vol 48 (supplement) ◽

pp. S22

Author(s):

Shigehumi Tadokoro ◽

Hironari Kamikubo ◽

Shigeo Yamaguchi ◽

Yoichi Yamazaki ◽

Mikio Kataoka

Keyword(s):

Catalytic Activity ◽

Annual Meeting ◽

Staphylococcal Nuclease ◽

Flexible Loop ◽

Biophysical Society

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3M1515 Role of 140Trp on Staphylococcal nuclease for structure

Seibutsu Butsuri ◽

10.2142/biophys.42.s193_2 ◽

2002 ◽

Vol 42 (supplement2) ◽

pp. S193

Author(s):

S. Hirano ◽

H. Kamikubo ◽

Y. Yamazaki ◽

Y. Imamoto ◽

M. Kataoka

Keyword(s):

Staphylococcal Nuclease

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3P019 The role of the flexible loop in Staphylococcal nuclease on its catalytic activity(01A. Protein: Structure,Poster)

Seibutsu Butsuri ◽

10.2142/biophys.53.s215_1 ◽

2013 ◽

Vol 53 (supplement1-2) ◽

pp. S215

Author(s):

Rumi Shiba ◽

Hironari Kamikubo ◽

Yutaka Maruyama ◽

Junko Yunoki ◽

Keiichi Fukuyama ◽

...

Keyword(s):

Catalytic Activity ◽

Protein Structure ◽

Staphylococcal Nuclease ◽

Flexible Loop

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Genetic control of the immune response to staphylococcal nuclease. IV. H-2-linked control of the relative proportions of antibodies produced to different determinants of native nuclease.

Journal of Experimental Medicine ◽

10.1084/jem.145.1.123 ◽

1977 ◽

Vol 145 (1) ◽

pp. 123-135 ◽

Cited By ~ 45

Author(s):

J A Berzofsky ◽

A N Schechter ◽

G M Shearer ◽

D H Sachs

Keyword(s):

Immune Response ◽

B Cells ◽

Antibody Response ◽

Binding Capacity ◽

Staphylococcal Nuclease ◽

Gene Control ◽

Low Responder ◽

Selection Of ◽

Ir Genes

The relative proportions of antibodies of different specificities within antisera raised to native staphylococcal nuclease have been studied in several strains of mice in which the antibody response has been shown to be under H-2-linked Ir-gene control. A method was developed in which binding to different radiolabeled fragments of nuclease was titrated against increasing fragment concentration until the binding capacity of the antiserum for that fragment was saturated. In comparing the low responder (H-2b) strain C57BL/10 with its congenic high responder counterpart B10.A (H-2a), it was found that the two strains made markedly and reproducibly different proportions of antibodies to different determinants on native nuclease. Since these two strains differ only at H-2, and therefore have identical immunoglobulin structural gene repertoires, we conclude that H-2-linked Ir genes can control the response to different determinants on the same antigen molecule independently of one another. This result suggests a possible role of H-2-linked genes in the selection of specific B cells.

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