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Cited by 264interferon and immune responsesImmune Response and InflammationImmunotherapy and Immune Responses

The DOI matches its Crossref record; 140 of the 140 references it cites were found in a registry or an index.

The IRF family of transcription factors: Inception, impact and implications in oncogenesis

Open access
Yanai, Hideyuki, Negishi, Hideo, Taniguchi, Tadatsugu·2012·OncoImmunology
DOI 10.4161/onci.22475PMC PMC3518510
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Abstract

Members of the interferon-regulatory factor (IRF) proteins family were originally identified as transcriptional regulators of the Type I interferon system. Thanks to consistent advances made in our understanding of the immunobiology of innate receptors, it is now clear that several IRFs are critical for the elicitation of innate pattern recognition receptors, and-as a consequence-for adaptive immunity. In addition, IRFs have attracted great attentions as they modulate cellular responses that are involved in tumorigenesis. The regulation of oncogenesis by IRFs has important implications for understanding the host susceptibility to several Types of cancers, their progression, as well as the potential for therapeutic interventions.

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Crossref · 10.4161/onci.22475

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Figures

Figure 1. Schematic illustration of human and viral IRF family members. Nine human IRF family members (IRF1 to IRF9) (upper) and three vIRFs (vIRF1, vIRF2, and vIRF3) (lower), all encoded by Kaposi sarcoma-associated herpesvirus (KSHV) are shown. Length (in amino acid) is reported. IRF family members possess an amino N-terminal DNA-binding domain (DBD) that is characterized by a series of five relatively well conserved tryptophan-rich repeats. All IRF family members, except for IRF1 and IRF2, contain an IRF association domain (IAD1). IRF1 and IRF2 share another IRF association domain (IAD2), which is structurally distinct from IAD1. IRF3 and IRF7 have multiple sites that—upon viral infection—are substrates for phosphorylation by the serine/threonine kinases TANK-binding kinase 1 (TBK1) and IκB kinase ε (IKKε). Phosphorylation at these sites is required for the nuclear translocation of IRF3 and IRF7. KSHV encodes a cluster of three viral vIRFs, all of which show homology in their N-terminal regions to the DBD of IRFs but lack several tryptophan residues. For this reason, vIRFs are believed to be unable to directly bind DNA. vIRF1 contains an IAD domain which enables vIRF1 to associate with other IRFs, such as IRF1. vIRF3 has an IAD-like domain which shows 32% identity with the IAD of IFR4, although the exact function of this domain remains elusive.
Figure 1. Schematic illustration of human and viral IRF family members. Nine human IRF family members (IRF1 to IRF9) (upper) and three vIRFs (vIRF1, vIRF2, and vIRF3) (lower), all encoded by Kaposi sarcoma-associated herpesvirus (KSHV) are shown. Length (in amino acid) is reported. IRF family members possess an amino N-terminal DNA-binding domain (DBD) that is characterized by a series of five relatively well conserved tryptophan-rich repeats. All IRF family members, except for IRF1 and IRF2, contain an IRF association domain (IAD1). IRF1 and IRF2 share another IRF association domain (IAD2), which is structurally distinct from IAD1. IRF3 and IRF7 have multiple sites that—upon viral infection—are substrates for phosphorylation by the serine/threonine kinases TANK-binding kinase 1 (TBK1) and IκB kinase ε (IKKε). Phosphorylation at these sites is required for the nuclear translocation of IRF3 and IRF7. KSHV encodes a cluster of three viral vIRFs, all of which show homology in their N-terminal regions to the DBD of IRFs but lack several tryptophan residues. For this reason, vIRFs are believed to be unable to directly bind DNA. vIRF1 contains an IAD domain which enables vIRF1 to associate with other IRFs, such as IRF1. vIRF3 has an IAD-like domain which shows 32% identity with the IAD of IFR4, although the exact function of this domain remains elusive.CC BY-NC · PubMed Central

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Research works printed but not linked: 9

  1. Tan RS, 1996, Cancer Res, 56, 2417
  2. Harada H, 1994, Oncogene, 9, 3313
  3. Tamura G, 1996, Cancer Res, 56, 612
  4. Nguyen H, 1995, Oncogene, 11, 537
  5. Yamamoto H, 1994, Oncogene, 9, 1423
  6. Oshita F, 2006, Oncol Rep, 16, 817
  7. Duguay D, 2002, Cancer Res, 62, 5148
  8. Barnes BJ, 2003, Cancer Res, 63, 6424
  9. Burysek L, 1999, J Hum Virol, 2, 19

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Metadata

Authors
Yanai, H., Negishi, H., & Taniguchi, T.
Affiliations
Japan Science and Technology Agency (JP)
Corresponding author
Taniguchi, Tadatsugu
ORCID
Venue
OncoImmunology
Publisher
Informa UK Limited
Published
2012-11
Volume
1
Issue
8
Pages
1376-1386
ISSN
  • 2162-4011 (ISSN-L)
  • 2162-402X
DOI
10.4161/onci.22475
PMC
PMC3518510
OpenAlex
W2031904443
Cited by
261
References
140
Citations by year
2026: 15 · 2025: 18 · 2024: 24 · 2023: 22 · 2022: 32 · 2021: 29 · 2020: 25 · 2019: 26 · 2018: 21 · 2017: 14 · 2016: 8 · 2015: 9 · 2014: 12 · 2013: 6
FWCI
3.78
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • OncoImmunology (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
Core Research for Evolutional Science and Technology
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
  • Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Keywords
interferon regulatory factors, transcription factors, type I interferon, innate immunity, pattern recognition receptors, adaptive immunity, carcinogenesis, cancer susceptibility, tumor progression, cancer therapy

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