Interferon regulatory factor gene transcriptions

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Associate Editor(s)-in-Chief: Henry A. Hoff

Interferon regulatory factors (IRF) are proteins which regulate transcription of interferons (see regulation of gene expression).[1] They are used in the JAK-STAT signaling pathway.[2] Interferon regulatory factors contain a conserved N-terminal region of about 120 amino acids, which folds into a structure that binds specifically to the interferon consensus sequence (ICS), which is located upstream of the interferon genes.[3] The remaining parts of the interferon regulatory factor sequence vary depending on the precise function of the protein.[3] The Kaposi sarcoma herpesvirus, KSHV[4], is a cancer virus that encodes four different IRF-like genes[5]; including vIRF1[6], which is a transforming oncoprotein that inhibits type 1 interferon activity.[7] In addition, the expression of IRF genes is under epigenetic regulation by promoter DNA methylation. [8]

Gene expressions

Main article: Gene expressions

IRF1

Interferon regulatory factor 1 is a protein that in humans is encoded by the IRF1 gene.[9][10]

Interferon regulatory factor 1 was the first member of the interferon regulatory transcription factor (IRF) family identified. Initially described as a transcription factor able to activate expression of the cytokine Interferon beta,[11] IRF-1 was subsequently shown to function as a transcriptional activator or repressor of a variety of target genes. IRF-1 regulates expression of target genes by binding to an interferon stimulated response element (ISRE) in their promoters. The IRF-1 protein binds to the ISRE via an N-terminal helix-turn-helix DNA binding domain,[12] which is highly conserved among all IRF proteins.

Beyond its function as a transcription factor, IRF-1 has also been shown to trans-activate the tumour suppressor protein p53 through the recruitment of its co-factor p300.[13]

IRF-1 has been shown to play roles in the immune response, regulating apoptosis, DNA damage and tumor suppression.[14]

It has been shown that the extreme C-terminus of IRF-1 regulates its ability to activate transcription, nanobodies targeting this domain (MF1) are able to increase IRF-1 activity.[15]

IRF2

Interferon regulatory factor 2 is a protein that in humans is encoded by the IRF2 gene.[16]

IRF2 encodes interferon regulatory factor 2, a member of the interferon regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of interferons alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4.[17]

IRF3

Interferon regulatory factor 3 (IRF3) is an interferon regulatory factor.[18]

IRF3 is a member of the interferon regulatory transcription factor (IRF) family.[18] IRF3 was originally discovered as a homolog of IRF1 and IRF2. IRF3 has been further characterized and shown to contain several functional domains including a nuclear export signal, a DNA-binding domain, a C-terminal IRF association domain and several regulatory phosphorylation sites.[19] IRF3 is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP.[20] This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes.[21]

IRF3 plays an important role in the innate immune system's response to viral infection.[22] Aggregated MAVS have been found to activate IRF3 dimerization.[23] A 2015 study shows phosphorylation of innate immune adaptor proteins MAVS, STING and TRIF at a conserved pLxIS motif recruits and specifies IRF3 phosphorylation and activation by the Serine/threonine-protein kinase TBK1, thereby activating the production of type-I interferons.[24] Another study has shown that IRF3-/- knockouts protect from myocardial infarction.[25] The same study identified IRF3 and the type I IFN response as a potential therapeutic target for post-myocardial infarction cardioprotection.[25]

IRF4

Interferon regulatory factor 4 also known as MUM1 is a protein that in humans is encoded by the IRF4 gene,[26][27][28] located at 6p25-p23.

In melanocytic cells the IRF4 gene may be regulated by MITF.[29] IRF4 is a transcription factor that has been implicated in acute leukemia.[30] This gene is strongly associated with pigmentation: sensitivity of skin to sun exposure, freckles, blue eyes, and brown hair color.[31] A variant has been implicated in greying of hair.[32]

IRF5

Interferon regulatory factor 5 is a protein that in humans is encoded by the IRF5 gene.[33]

IRF5 is a member of the interferon regulatory factor (IRF) family, a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Alternative splice variants encoding different isoforms exist.[34]

An adaptor protein named TASL plays an important regulatory role in IRF5 activation by being phosphorylated at the pLxIS motif,[35] drawing a similar analogy to the IRF3 activation pathway through the adaptor proteins MAVS, STING and TRIF.[36]

IRF6

Interferon regulatory factor 6 (IRF6) is a protein that in humans is encoded by the IRF6 gene.[37]

This gene encodes a member of the interferon regulatory transcription factor (IRF) family. Family members share a highly conserved N-terminal helix-turn-helix DNA-binding domain and a less conserved C-terminal protein-binding domain.[38] The function of IRF6 is related to the formation of connective tissue, for example that of the palate.[39] This gene encodes a member of the interferon regulatory transcription factor (IRF) family. In addition, it has been observed that IRF6 gene is under epigenetic regulation by promoter methylation.[8]

IRF7

Interferon regulatory factor 7 (IRF7) is a member of the interferon regulatory factor family of transcription factors.

IRF7 encodes interferon regulatory factor 7, a member of the interferon regulatory transcription factor (IRF) family. IRF7 has been shown to play a role in the transcriptional activation of virus-inducible cellular genes, including the type I interferon genes. In particular, IRF7 regulates many interferon-alpha genes.[40] Constitutive expression of IRF7 is largely restricted to lymphoid tissue, largely plasmacytoid dendritic cells, whereas IRF7 is inducible in many tissues. Multiple IRF7 transcript variants have been identified, although the functional consequences of these have not yet been established.[41]

The IRF7 pathway was shown to be silenced in some metastatic breast cancer cell lines, which may help the cells avoid the host immune response.[42] Restoring IRF7 to these cell lines reduced metastases and increased host survival time in animal models.

The IRF7 gene and product were shown to be defective in a patient with severe susceptibility to H1N1 influenza, while susceptibility to other viral diseases such as CMV, RSV, and parainfluenza was unaffected.[43]

IRF8

Interferon regulatory factor 8 (IRF8) also known as the interferon consensus sequence-binding protein (ICSBP), is a protein that in humans is encoded by the IRF8 gene.[44][3][45] IRF8 is a transcription factor that plays critical roles in the regulation of lineage commitment and in myeloid cell maturation including the decision for a common myeloid progenitor (CMP) to differentiate into a monocyte precursor cell.

Interferon Consensus Sequence-binding protein (ICSBP) is a transcription factor of the interferon regulatory factor (IRF) family. Proteins of this family are composed of a conserved DNA-binding domain in the N-terminal region and a divergent C-terminal region that serves as the regulatory domain. The IRF family proteins bind to the IFN-stimulated response element (ISRE) and regulate expression of genes stimulated by type I IFNs, namely IFN-α and IFN-β. IRF family proteins also control expression of IFN-α and IFN-β-regulated genes that are induced by viral infection.[34]

IRF9

Interferon regulatory factor 9 is a protein that in humans is encoded by the IRF9 gene, previously known as ISGF3G.[46][47][48]

Interactions

Main article: Interaction gene transcriptions

IRF1 has been shown to interact with:

IRF2 has been shown to interact with BRD7,[61] EP300[62] and PCAF.[62][56]

IRF3 has been shown to interact with IRF7.[63]

IRF4 has been shown to interact with:

IRF7 has been shown to interact with IRF3.[63] Also, IRF7 has been shown to interact with Aryl Hydrocarbon Receptor Interacting Protein (AIP), which is a negative regulator for the antiviral pathway.[68]

IRF8 has been shown to interact with IRF1[52][53] and COPS2.[69]

IRF9 has been shown to interact with STAT2[70][71] and STAT1.[70]

Consensus sequences

Main article: Consensus sequence gene transcriptions

Consensus sequence for IRF-3 is 5'-GCTTTCC-3'.[72]

Acknowledgements

The content on this page was first contributed by: Henry A. Hoff.

Initial content for this page in some instances came from Wikipedia.

See also

References

  1. ↑ Paun A, Pitha PM (2007). "The IRF family, revisited". Biochimie. 89 (6–7): 744–53. doi:10.1016/j.biochi.2007.01.014. PMC 2139905. PMID 17399883.
  2. ↑ Tsuneya Ikezu; Howard E. Gendelman (2008). Neuroimmune Pharmacology. Springer. pp. 213–. ISBN 978-0-387-72572-7. Retrieved 28 November 2010.
  3. ↑ 3.0 3.1 3.2 Weisz A, Marx P, Sharf R, Appella E, Driggers PH, Ozato K, Levi BZ (December 1992). "Human interferon consensus sequence binding protein is a negative regulator of enhancer elements common to interferon-inducible genes". J. Biol. Chem. 267 (35): 25589–96. PMID 1460054.
  4. ↑ Chang Y, Cesarman E, Pessin MS, Lee F, Culpepper J, Knowles DM, Moore PS (December 1994). "Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma". Science. 266 (5192): 1865–9. Bibcode:1994Sci...266.1865C. doi:10.1126/science.7997879. PMID 7997879.
  5. ↑ Offermann MK (2007). "Kaposi sarcoma herpesvirus-encoded interferon regulator factors". Curr Top Microbiol Immunol. Current Topics in Microbiology and Immunology. 312: 185–209. doi:10.1007/978-3-540-34344-8_7. ISBN 978-3-540-34343-1. PMID 17089798.
  6. ↑ Moore PS, Boshoff C, Weiss RA, Chang Y (December 1996). "Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV". Science. 274 (5293): 1739–44. Bibcode:1996Sci...274.1739M. doi:10.1126/science.274.5293.1739. PMID 8939871. Unknown parameter |s2cid= ignored (help)
  7. ↑ Gao SJ, Boshoff C, Jayachandra S, Weiss RA, Chang Y, Moore PS (October 1997). "KSHV ORF K9 (vIRF) is an oncogene which inhibits the interferon signaling pathway". Oncogene. 15 (16): 1979–85. doi:10.1038/sj.onc.1201571. PMID 9365244.
  8. ↑ 8.0 8.1 Rotondo JC, Borghi A, Selvatici R, Magri E, Bianchini E, Montinari E, Corazza M, Virgili A, Tognon M, Martini F (2016). "Hypermethylation-Induced Inactivation of the IRF6 Gene as a Possible Early Event in Progression of Vulvar Squamous Cell Carcinoma Associated With Lichen Sclerosus". JAMA Dermatology. 152 (8): 928–33. doi:10.1001/jamadermatol.2016.1336. PMID 27223861.
  9. ↑ Maruyama M, Fujita T, Taniguchi T (Jun 1989). "Sequence of a cDNA coding for human IRF-1". Nucleic Acids Res. 17 (8): 3292. doi:10.1093/nar/17.8.3292. PMC 317732. PMID 2726461.
  10. ↑ Itoh S, Harada H, Nakamura Y, White R, Taniguchi T (Nov 1991). "Assignment of the human interferon regulatory factor-1 (IRF1) gene to chromosome 5q23-q31". Genomics. 10 (4): 1097–9. doi:10.1016/0888-7543(91)90208-V. PMID 1680796.
  11. ↑ Miyamoto M, Fujita T, Kimura Y, Maruyama M, Harada H, Sudo Y, Miyata T, Taniguchi T (September 1988). "Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-beta gene regulatory elements". Cell. 54 (6): 903–13. doi:10.1016/S0092-8674(88)91307-4. PMID 3409321. Unknown parameter |s2cid= ignored (help)
  12. ↑ Escalante CR, Yie J, Thanos D, Aggarwal AK (January 1998). "Structure of IRF-1 with bound DNA reveals determinants of interferon regulation". Nature. 391 (6662): 103–6. Bibcode:1998Natur.391..103E. doi:10.1038/34224. PMID 9422515. Unknown parameter |s2cid= ignored (help)
  13. ↑ Dornan D, Eckert M, Wallace M, Shimizu H, Ramsay E, Hupp TR, Ball KL (November 2004). "Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53". Mol. Cell. Biol. 24 (22): 10083–98. doi:10.1128/MCB.24.22.10083-10098.2004. PMC 525491. PMID 15509808.
  14. ↑ "Entrez Gene: IRF1 interferon regulatory factor 1".
  15. ↑ Möller A, Pion E, Narayan V, Ball KL (December 2010). "Intracellular activation of interferon regulatory factor-1 by nanobodies to the multifunctional (Mf1) domain". J. Biol. Chem. 285 (49): 38348–61. doi:10.1074/jbc.M110.149476. PMC 2992268. PMID 20817723.
  16. ↑ Harada H, Fujita T, Miyamoto M, Kimura Y, Maruyama M, Furia A, Miyata T, Taniguchi T (September 1989). "Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes". Cell. 58 (4): 729–39. doi:10.1016/0092-8674(89)90107-4. PMID 2475256. Unknown parameter |s2cid= ignored (help)
  17. ↑ "Entrez Gene: IRF2 interferon regulatory factor 2".
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  19. ↑ Lin R, Heylbroeck C, Genin P, Pitha PM, Hiscott J (Feb 1999). "Essential Role of Interferon Regulatory Factor 3 in Direct Activation of RANTES Chemokine Transcription". Mol Cell Biol. 19 (2): 959–66. doi:10.1128/MCB.19.2.959. PMC 116027. PMID 9891032.
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  22. ↑ Collins SE, Noyce RS, Mossman KL (Feb 2004). "Innate Cellular Response to Virus Particle Entry Requires IRF3 but Not Virus Replication". J Virol. 78 (4): 1706–17. doi:10.1128/JVI.78.4.1706-1717.2004. PMC 369475. PMID 14747536.
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  25. ↑ 25.0 25.1 King KR, Aguirre AD, Ye YX, Sun Y, Roh JD, Ng Jr RP, Kohler RH, Arlauckas SP, Iwamoto Y, Savol A, Sadreyev RI, Kelly M, Fitzgibbons TP, Fitzgerald KA, Mitchison T, Libby P, Nahrendorf M, Weissleder R (Nov 6, 2017). "IRF3 and type I interferons fuel a fatal response to myocardial infarction". Nature Medicine. 23 (12): 1481–1487. doi:10.1038/nm.4428. PMC 6477926. PMID 29106401.
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  34. ↑ 34.0 34.1
  35. ↑ Heinz, Leonhard X.; Lee, JangEun; Kapoor, Utkarsh; Kartnig, Felix; Sedlyarov, Vitaly; Papakostas, Konstantinos; César-Razquin, Adrian; Essletzbichler, Patrick; Goldmann, Ulrich; Stefanovic, Adrijana; Bigenzahn, Johannes W.; Scorzoni, Stefania; Pizzagalli, Mattia D.; Bensimon, Ariel; Müller, André C.; King, F. James; Li, Jun; Girardi, Enrico; Mbow, M. Lamine; Whitehurst, Charles E.; Rebsamen, Manuele; Superti-Furga, Giulio (13 May 2020). "TASL is the SLC15A4-associated adaptor for IRF5 activation by TLR7–9". Nature. 581 (7808): 316–322. Bibcode:2020Natur.581..316H. doi:10.1038/s41586-020-2282-0. PMID 32433612 Check |pmid= value (help). Unknown parameter |s2cid= ignored (help)
  36. ↑ Liu S, Cai X, Wu J, Cong Q, Chen X, Li T, Du F, Ren J, Wu Y, Grishin N, and Chen ZJ (Mar 13, 2015). "Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation". Science. 347 (6227): aaa2630. doi:10.1126/science.aaa2630. PMID 25636800.
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  38. ↑ "Entrez Gene: IRF6".
  39. ↑ Blanton SH, Cortez A, Stal S, Mulliken JB, Finnell RH, Hecht JT (September 2005). "Variation in IRF6 contributes to nonsyndromic cleft lip and palate". Am. J. Med. Genet. A. 137A (3): 259–62. doi:10.1002/ajmg.a.30887. PMID 16096995. Unknown parameter |s2cid= ignored (help)
  40. ↑ Marié I, Durbin JE, Levy DE (November 1998). "Differential viral induction of distinct interferon-alpha genes by positive feedback through interferon regulatory factor-7". The EMBO Journal. 17 (22): 6660–9. doi:10.1093/emboj/17.22.6660. PMC 1171011. PMID 9822609.
  41. ↑ "Entrez Gene: IRF7 interferon regulatory factor 7".
  42. ↑ Bidwell (2012). "Silencing of Irf7 pathways in breast cancer cells promotes bone metastasis through immune escape". Nature Medicine. 18 (8): 1224–1231. doi:10.1038/nm.2830. PMID 22820642. Unknown parameter |s2cid= ignored (help)
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  48. ↑ "Entrez Gene: ISGF3G interferon-stimulated transcription factor 3, gamma 48kDa".
  49. ↑ Narayan V, Pion E, Landré V, Müller P, Ball KL (October 2010). "Docking dependent ubiquitination of the interferon regulatory factor-1 tumour suppressor protein by the ubiquitin ligase CHIP". J Biol Chem. 286 (1): 607–19. doi:10.1074/jbc.M110.153122. PMC 3013021. PMID 20947504.
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  72. ↑ Jianyin Long, Daniel L. Galvan, Koki Mise, Yashpal S. Kanwar, Li Li, Naravat Poungavrin, Paul A. Overbeek, Benny H. Chang, and Farhad R. Danesh (28 May 2020). "Role for carbohydrate response element-binding protein (ChREBP) in high glucose-mediated repression of long noncoding RNA Tug1" (PDF). Journal of Biological Chemistry. 5 (28). doi:10.1074/jbc.RA120.013228. Retrieved 6 October 2020.

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