IL37, IL37(?-218) translocates from cytosol to extracellular region

Stable Identifier
Reaction [transition]
Homo sapiens
IL-37, IL-37(?-218) translocates from cytosol to extracellular region
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Interleukins (IL) are immunomodulatory proteins that elicit a wide array of responses in cells and tissues. Interleukin 37 (IL-37, IL-1 F7) is a member of the IL-1 family. There are five isoforms of IL-37 (a-e) of which transcript IL-37b is known to be functional (Sharma et al. 2008). This isoform is represented in UniProt as the canonical form of IL-37 and in Reactome as the full length, unprocessed form of IL-37. Like several other IL-1 family members, IL-37 is synthesized as a precursor that requires processing (primarily by caspase 1) to attain full receptor agonist or antagonist function. The putative caspase 1 cleavage site is at aspartic acid 20 (Kumar et al. 2002). Both full length and cleaved IL-37 can be secreted from the cytosol to the extracellular space via a mechanism dependent on caspase 1 cleavage of IL-37 (Bulau A M et al. 2014).
Literature References
PubMed ID Title Journal Year
24481253 Role of caspase-1 in nuclear translocation of IL-37, release of the cytokine, and IL-37 inhibition of innate immune responses

Dinarello, CA, Bufler, P, Li, S, Rubartelli, A, Fink, M, Bulau, AM, Schwerd, T, Mansell, A, Nold, MF, Hong, J, Nold-Petry, CA

Proc. Natl. Acad. Sci. U.S.A. 2014
Orthologous Events
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