| http://purl.uniprot.org/citations/22203669 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22203669 | http://www.w3.org/2000/01/rdf-schema#comment | "IL-32 can be expressed in several isoforms. The amino acid sequences of the major IL-32 isoforms were used to predict the secondary and tertiary protein structure by I-TASSER software. The secondary protein structure revealed coils and α-helixes, but no β sheets. Furthermore, IL-32 contains an RGD motif, which potentially activates procaspase-3 intracellular and or binds to integrins. Mutation of the RGD motif did not result in inhibition of the IL-32β- or IL-32γ-induced cytotoxicity mediated through caspase-3. Although IL-32α interacted with the extracellular part of αVβ3 and αVβ6 integrins, only the αVβ3 binding was inhibited by small RGD peptides. Additionally, IL-32β was able to bind to αVβ3 integrins, whereas this binding was not inhibited by small RGD peptides. In addition to the IL-32/integrin interactions, we observed that IL-32 is also able to interact with intracellular proteins that are involved in integrin and focal adhesion signaling. Modeling of IL-32 revealed a distinct α-helix protein resembling the focal adhesion targeting region of focal adhesion kinase (FAK). Inhibition of FAK resulted in modulation of the IL-32β- or IL-32γ-induced cytotoxicity. Interestingly, IL-32α binds to paxillin without the RGD motif being involved. Finally, FAK inhibited IL-32α/paxillin binding, whereas FAK also could interact with IL-32α, demonstrating that IL-32 is a member of the focal adhesion protein complex. This study demonstrates for the first time that IL-32 binds to the extracellular domain of integrins and to intracellular proteins like paxillin and FAK, suggesting a dual role for IL-32 in integrin signaling."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.288290"xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/author | "Netea M.G."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/author | "Dinarello C.A."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/author | "Joosten L.A."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/author | "van den Berg W.B."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/author | "Koenders M.I."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/author | "Heinhuis B."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/pages | "5733-5743"xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/title | "Interleukin 32 (IL-32) contains a typical alpha-helix bundle structure that resembles focal adhesion targeting region of focal adhesion kinase-1."xsd:string |
| http://purl.uniprot.org/citations/22203669 | http://purl.uniprot.org/core/volume | "287"xsd:string |
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