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Shi Y, Castro-Gonzalez S, Chen Y, et al. Effects of the SUMO Ligase BCA2 on Metabolic Activity, Cell Proliferation, Cell Migration, Cell Cycle, and the Regulation of NF-κB and IRF1 in Different Breast Epithelial Cellular Contexts. Front Cell Dev Biol. 2021;9:711481doi: 10.3389/fcell.2021.711481.
Shi, Y., Castro-Gonzalez, S., Chen, Y., & Serra-Moreno, R. (2021). Effects of the SUMO Ligase BCA2 on Metabolic Activity, Cell Proliferation, Cell Migration, Cell Cycle, and the Regulation of NF-κB and IRF1 in Different Breast Epithelial Cellular Contexts. Frontiers in cell and developmental biology, 9711481. https://doi.org/10.3389/fcell.2021.711481
Shi, Yuhang, et al. "Effects of the SUMO Ligase BCA2 on Metabolic Activity, Cell Proliferation, Cell Migration, Cell Cycle, and the Regulation of NF-κB and IRF1 in Different Breast Epithelial Cellular Contexts." Frontiers in cell and developmental biology vol. 9 (2021): 711481. doi: https://doi.org/10.3389/fcell.2021.711481
Shi Y, Castro-Gonzalez S, Chen Y, Serra-Moreno R. Effects of the SUMO Ligase BCA2 on Metabolic Activity, Cell Proliferation, Cell Migration, Cell Cycle, and the Regulation of NF-κB and IRF1 in Different Breast Epithelial Cellular Contexts. Front Cell Dev Biol. 2021 Sep 13;9:711481. doi: 10.3389/fcell.2021.711481. eCollection 2021. PMID: 34589482; PMCID: PMC8473798.
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Front Cell Dev Biol. 2021 Sep 13;9:711481. doi: 10.3389/fcell.2021.711481. eCollection 2021.

Effects of the SUMO Ligase BCA2 on Metabolic Activity, Cell Proliferation, Cell Migration, Cell Cycle, and the Regulation of NF-κB and IRF1 in Different Breast Epithelial Cellular Contexts.

Frontiers in cell and developmental biology

Yuhang Shi, Sergio Castro-Gonzalez, Yuexuan Chen, Ruth Serra-Moreno

Affiliations

  1. Microbiology and Immunology, University of Rochester Medical Center, Rochester, NY, United States.
  2. Department of Chemistry, Umeå University, Umeå, Sweden.

PMID: 34589482 PMCID: PMC8473798 DOI: 10.3389/fcell.2021.711481

Abstract

Breast cancer-associated gene 2 (BCA2) is an E3 ubiquitin and SUMO ligase with antiviral properties against HIV. Specifically, BCA2 (i) enhances the restriction imposed by BST2/Tetherin, impeding viral release; (ii) promotes the ubiquitination and degradation of the HIV protein Gag, limiting virion production; (iii) down-regulates NF-κB, which is necessary for HIV RNA synthesis; and (iv) activates the innate transcription factor IRF1. Due to its antiviral properties, ectopic expression of BCA2 in infected cells represents a promising therapeutic approach against HIV infection. However, BCA2 up-regulation is often observed in breast tumors. To date, the studies about BCA2 and cancer development are controversial, stating both pro- and anti-oncogenic roles. Here, we investigated the impact of BCA2 on cellular metabolic activity, cell proliferation, cell migration, and cell cycle progression. In addition, we also examined the ability of BCA2 to regulate NF-κB and IRF1 in transformed and non-tumor breast epithelial environments. Despite the fact that BCA2 promotes the transition from G1 to S phase of the cell cycle, it did not increase cell proliferation, migration nor metabolic activity. As expected, BCA2 maintains its enzymatic function at inhibiting NF-κB in different breast cancer cell lines. However, the effect of BCA2 on IRF1 differs depending on the cellular context. Specifically, BCA2 activates IRF1 in ER

Copyright © 2021 Shi, Castro-Gonzalez, Chen and Serra-Moreno.

Keywords: BCA2; IRF1; NF-κB; antiviral defense; cancer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

References

  1. Cell Host Microbe. 2008 Apr 17;3(4):245-52 - PubMed
  2. DNA Repair (Amst). 2016 Jun;42:63-71 - PubMed
  3. J Clin Invest. 2012 Mar;122(3):859-72 - PubMed
  4. Mol Cancer Res. 2008 Sep;6(9):1385-96 - PubMed
  5. PLoS One. 2013 Jul 30;8(7):e68425 - PubMed
  6. Cancer Res. 2005 Nov 15;65(22):10401-12 - PubMed
  7. J Cancer. 2016 Dec 9;7(15):2388-2407 - PubMed
  8. Int J Mol Med. 2018 Jun;41(6):3366-3378 - PubMed
  9. Br J Cancer. 2013 Jul 9;109(1):76-82 - PubMed
  10. J Virol. 2017 Mar 29;91(8): - PubMed
  11. J Virol. 2001 Sep;75(18):8524-37 - PubMed
  12. Open Cancer J. 2010;3(1):116-123 - PubMed
  13. Cancer Immunol Res. 2014 Sep;2(9):823-30 - PubMed
  14. Neoplasia. 2006 Aug;8(8):689-95 - PubMed
  15. Carcinogenesis. 2005 Sep;26(9):1527-35 - PubMed
  16. Biochim Biophys Acta. 2015 May;1849(5):506-16 - PubMed
  17. Oncogene. 2006 Oct 30;25(51):6758-80 - PubMed
  18. J Cell Sci. 2013 Mar 15;126(Pt 6):1366-80 - PubMed
  19. J Mol Med (Berl). 1996 Dec;74(12):749-69 - PubMed
  20. Eur J Cancer. 2002 Jul;38(10):1329-34 - PubMed
  21. Genes Dev. 1992 May;6(5):761-74 - PubMed
  22. PLoS One. 2012;7(7):e41891 - PubMed
  23. J Clin Oncol. 2003 May 15;21(10):1973-9 - PubMed
  24. Mol Cell Endocrinol. 2015 Dec 15;418 Pt 3:235-9 - PubMed
  25. Nature. 1987 Apr 16-22;326(6114):711-3 - PubMed
  26. PLoS Pathog. 2021 Jan 21;17(1):e1009220 - PubMed
  27. Nature. 2008 Jan 24;451(7177):425-30 - PubMed
  28. Genes Dev. 2004 Sep 15;18(18):2195-224 - PubMed
  29. Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):17028-33 - PubMed
  30. Nat Commun. 2017 Mar 20;8:14728 - PubMed
  31. PLoS Pathog. 2014 May 22;10(5):e1004151 - PubMed
  32. Cold Spring Harb Perspect Biol. 2009 Oct;1(4):a000034 - PubMed
  33. Cell Biochem Funct. 2013 Apr;31(3):263-8 - PubMed
  34. Neoplasia. 2013 Sep;15(9):1028-35 - PubMed
  35. Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):10137-42 - PubMed
  36. PLoS Pathog. 2009 Dec;5(12):e1000700 - PubMed
  37. Cell Rep. 2015 Apr 7;11(1):98-110 - PubMed
  38. Cell Host Microbe. 2012 Feb 16;11(2):181-93 - PubMed
  39. Mol Cancer. 2013 Aug 02;12:86 - PubMed
  40. Breast Cancer Res. 2007;9(1):R6 - PubMed
  41. Nat Rev Cancer. 2009 Jun;9(6):400-14 - PubMed

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