Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses.

By Wen Yong Chen, David H. Wang, Ray-Whay Chiu Yen, Jianyuan Luo, W. Gu, S. Baylin. Cell, 2005

681 citations recorded by the source corpus.

Subfields: Epidemiology, Geriatrics and Gerontology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/da3dbf48c8adec6aa32869d78b4a895eb2c8cb9c

How researchers see this paper

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In Epidemiology

1. D. Sinclair
2. E. Verdin
3. Peter A. Jones
4. L. Guarente

In Geriatrics and Gerontology

1. D. Sinclair
2. L. Guarente
3. E. Verdin
4. C. Deng
5. S. Baylin
6. L. Saunders
7. G. Blander
8. Shaday Michán

In Molecular Biology

1. Peter A. Jones
2. Manel Esteller
3. S. Baylin
4. D. Sinclair
5. E. Verdin
6. S. Ropero
7. Joyce Ohm
8. G. Blander

Citations in the corpus

• Epigenetic gene silencing in cancer – a mechanism for early oncogenic pathway addiction? (2006, background): “How do we account for this interaction? One way in which HIC1 seems to function as a tumour suppressor involves its ability to directly repress transcription of the cell-stress-sensing protein SIRT1 (Ref”
• Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice (2008, positive): “For example, the observation that SIRT1 deacetylates p53 to decrease its activity has led to the hypothesis that increased SIRT1 activity may elevate cancer risk in mammals (Chen et al., 2005).”
• miR-34a repression of SIRT1 regulates apoptosis (2008, background): “Increased expression of SIRT1 in normal or cancer cells inactivates p53, decreasing cellular apoptosis (58).”
• Regulation of SIRT1 and Its Roles in Inflammation (2022, background): “HIC1 binds to SIRT1 and C-terminal binding protein 1 (CTBP1), forming an inhibition complex that represses SIRT1 expression by interacting with enhancer elements upstream of the SIRT1 promoter (32).”
• The SIRT1 Deacetylase Suppresses Intestinal Tumorigenesis and Colon Cancer Growth (2008, background): “the tumor suppressor gene, HIC1 [6], can inhibit apoptosis [7,8,9,10] and down-regulates the expression of tumor suppressor genes [11], leading many to conclude that SIRT1 will prove to be an oncogene in vivo.”
• Sirtuins: critical regulators at the crossroads between cancer and aging (2007, background): “Similar to the intimate feedback loop with E2F1, SIRT1 interacts with HIC1 and represses its own expression (Chen et al., 2005).”
• Epigenetic Determinants of Cancer. (2016, background): “It complements p53 mutations (Chen et al. 2003) leading to upregulation of SIRT1 (Chen et al. 2005), which contributes to enhanced stem/progenitor cell growth (Howitz et al. 2003; Nemoto et al. 2004; Kuzmichev et al. 2005).”
• NAD+/NADH and NADP+/NADPH in Cellular Functions and Cell Death: Regulation and Biological Consequences (2008, neutral): “indicated that SIRT1 inhibition by tumor suppressor HIC1 in human MCF-7 cancer cells mediates DNA damage-induced apoptosis by both producing p53 acetylation and suppressing the antiapoptotic factor bcl-2 (52).”
• Multiple functions of p21 in cell cycle, apoptosis and transcriptional regulation after DNA damage. (2016, background): “HIC1 downegulates SIRT1 transcription [50], whereas SIRT1 strengthens the IC1 by deacetylating the Lys-314 of HIC1 [51].”
• The role of histone deacetylases (HDACs) in human cancer (2007, background): “The lost of HDAC2 function could induce the hyperacetylation and reexpression of genes regulated by retinoblastoma protein Rb, and with crucial functions in cell cycle regulation. functions of this protein (Chen et al., 2005).”
• The epigenomics of cancer. (2007, background): “HIC1, a transcriptional repressor complexed with SIRT1, can downmodulate SIRT1 promoter activity (Chen et al., 2005).”
• SIRTUIN 1 AND SIRTUIN 3: PHYSIOLOGICAL MODULATORS OF METABOLISM (2012, background): “HIC1, COOH-terminal binding protein 1 (CTBP1), and SIRT1 form a corepressor complex (76) that binds enhancer elements upstream of the SIRT1 promoter and inhibits SIRT1 expression.”