IL37(?-218) binds p-S423,S425-SMAD3

Stable Identifier
Reaction [binding]
Homo sapiens
IL-37(?-218) binds p-S423,S425-SMAD3
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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). Mothers against decapentaplegic homolog 3 (SMAD3) binds SMAD4 and this complex modulates the transcription of several genes downstream. IL-37(? 218) can bind phosphorylated SMAD3 in A549 cells (Nold M F et al. 2010, Grimsby S et al. 2004) and may affect its function.
Literature References
PubMed ID Title Journal Year
20935647 IL-37 is a fundamental inhibitor of innate immunity

Dinarello, CA, Bufler, P, Nold, MF, Nold-Petry, CA, Palmer, BE, Zepp, JA

Nat. Immunol. 2010
15527767 Proteomics-based identification of proteins interacting with Smad3: SREBP-2 forms a complex with Smad3 and inhibits its transcriptional activity

Jaensson, H, Souchelnytskyi, S, Lomnytska, M, Hellman, U, Dubrovska, A, Grimsby, S

FEBS Lett. 2004
Orthologous Events
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