Type II cytokine receptor

Today, Type II cytokine receptor is a topic that generates great interest and debate in society. For years, Type II cytokine receptor has been the object of study, analysis and reflection by experts and scientists in different areas. Its relevance has been reflected in numerous studies, conferences and publications that seek to understand its impact and scope in different contexts. Type II cytokine receptor is a topic that crosses borders and reaches people of different ages, genders, cultures and nationalities, generating an enriching dialogue that allows us to understand it from different perspectives. In this article, we will delve into the world of Type II cytokine receptor, exploring its origin, evolution and consequences in today's society. Through interviews, analysis and testimonies, we will give a voice to those who have been impacted by Type II cytokine receptor and delve into its global implications.

Type II cytokine receptor
Identifiers
SymbolType II cytokine receptor
Pfam clanCL0159
Membranome2
Interferon gamma receptor
Identifiers
SymbolIFNGR1
PfamPF07140
InterProIPR021126
SCOP21fg9 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Interferon-alpha/beta receptor, fibronectin type III
Identifiers
SymbolInterfer-bind
PfamInterfer-bind
InterProIPR015373
SCOP21n6u / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Type II cytokine receptors, also commonly known as class II cytokine receptors, are transmembrane proteins that are expressed on the surface of certain cells. They bind and respond to a select group of cytokines including interferon type I, interferon type II, interferon type III.[1] and members of the interleukin-10 family[2][3] These receptors are characterized by the lack of a WSXWS motif which differentiates them from type I cytokine receptors.[4]

Structure

Typically type II cytokine receptors are heterodimers or multimers with a high and a low affinity component. These receptors are related predominantly by sequence similarities in their extracellular portions that are composed of tandem Ig-like domains. The structures for the extracellular domains of the receptors for interferon types, I, II, and III are all known.[5]

Type II cytokine receptors are tyrosine-kinase-linked receptors. The intracellular domain of type II cytokine receptors is typically associated with a tyrosine kinase belonging to the Janus kinase (JAK family). Binding of the receptor typically leads to activation of the canonical JAK/STAT signaling pathway.[6]

Types

Type II cytokine receptors include those that bind interferons and those that bind members of the interleukin-10 family (interleukin-10, interleukin-20, interleukin-22, and interleukin-28).[3][2] Expression of specific receptor varieties is highly variable across tissue types with some receptors being ubiquitously expressed and some receptors only expressed in specific tissues.[4]

Interferon receptors

The interferon receptor is a molecule displayed on the surface of cells which interacts with extracellular interferons. Class II cytokine receptors bind type I, type II, and type III interferons. Type I interferons play important roles in both the adaptive and innate immune responses, prevent proliferation of pathogens, and have antiviral activities. Type II interferons help to modulate the immune system’s response to pathogens, and these interferons also respond to pathogens. Type III interferons induce a similar response to type I interferons, but their expression is limited to epithelial cells.[1][4] The receptor is coded for by number of different genes, due to the diversity of types of interferons. Regulation of cell surface receptor levels plays an important role in the regulation and limiting of interferon signaling.

Interleukin receptors

References

  1. ^ a b Krey K, Babnis AW, Pichlmair A (October 2020). "System-Based Approaches to Delineate the Antiviral Innate Immune Landscape". Viruses. 12 (10): 1196. doi:10.3390/v12101196. PMC 7589202. PMID 33096788.
  2. ^ a b Xu W, Presnell SR, Parrish-Novak J, Kindsvogel W, Jaspers S, Chen Z, et al. (August 2001). "A soluble class II cytokine receptor, IL-22RA2, is a naturally occurring IL-22 antagonist". Proceedings of the National Academy of Sciences of the United States of America. 98 (17): 9511–6. Bibcode:2001PNAS...98.9511X. doi:10.1073/pnas.171303198. PMC 55483. PMID 11481447.
  3. ^ a b Dumoutier L, Lejeune D, Hor S, Fickenscher H, Renauld JC (March 2003). "Cloning of a new type II cytokine receptor activating signal transducer and activator of transcription (STAT)1, STAT2 and STAT3". The Biochemical Journal. 370 (Pt 2): 391–6. doi:10.1042/BJ20021935. PMC 1223207. PMID 12521379.
  4. ^ a b c Stanifer ML, Pervolaraki K, Boulant S (March 2019). "Differential Regulation of Type I and Type III Interferon Signaling". International Journal of Molecular Sciences. 20 (6): 1445. doi:10.3390/ijms20061445. PMC 6471306. PMID 30901970.
  5. ^ Walter MR (2020). "The Role of Structure in the Biology of Interferon Signaling". Frontiers in Immunology. 11: 606489. doi:10.3389/fimmu.2020.606489. PMC 7689341. PMID 33281831.
  6. ^ Fox LE, Locke MC, Lenschow DJ (2020-12-21). "Context Is Key: Delineating the Unique Functions of IFNα and IFNβ in Disease". Frontiers in Immunology. 11: 606874. doi:10.3389/fimmu.2020.606874. PMC 7779635. PMID 33408718.