dc.date.accessioned | 2018-01-23T13:43:20Z | |
dc.date.available | 2018-01-23T13:43:20Z | |
dc.date.created | 2017-12-20T12:51:48Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Imre, Gergely Berthelet, Jean Heering, Jan Kehrloesser, Sebastian Melzer, Inga Maria Lee, Byung Il Thiede, Bernd Dötsch, Volker Rajalingam, Krishnaraj . Apoptosis inhibitor 5 is an endogenous inhibitor of caspase-2. EMBO Reports. 2017, 18(5), 733-744 | |
dc.identifier.uri | http://hdl.handle.net/10852/59674 | |
dc.description.abstract | Caspases are key enzymes responsible for mediating apoptotic cell death. Across species, caspase‐2 is the most conserved caspase and stands out due to unique features. Apart from cell death, caspase‐2 also regulates autophagy, genomic stability and ageing. Caspase‐2 requires dimerization for its activation which is primarily accomplished by recruitment to high molecular weight protein complexes in cells. Here, we demonstrate that apoptosis inhibitor 5 (API5/AAC11) is an endogenous and direct inhibitor of caspase‐2. API5 protein directly binds to the caspase recruitment domain (CARD) of caspase‐2 and impedes dimerization and activation of caspase‐2. Interestingly, recombinant API5 directly inhibits full length but not processed caspase‐2. Depletion of endogenous API5 leads to an increase in caspase‐2 dimerization and activation. Consistently, loss of API5 sensitizes cells to caspase‐2‐dependent apoptotic cell death. These results establish API5/AAC‐11 as a direct inhibitor of caspase‐2 and shed further light onto mechanisms driving the activation of this poorly understood caspase. | en_US |
dc.language | EN | |
dc.publisher | Nature Publishing Group | |
dc.title | Apoptosis inhibitor 5 is an endogenous inhibitor of caspase-2 | en_US |
dc.type | Journal article | en_US |
dc.creator.author | Imre, Gergely | |
dc.creator.author | Berthelet, Jean | |
dc.creator.author | Heering, Jan | |
dc.creator.author | Kehrloesser, Sebastian | |
dc.creator.author | Melzer, Inga Maria | |
dc.creator.author | Lee, Byung Il | |
dc.creator.author | Thiede, Bernd | |
dc.creator.author | Dötsch, Volker | |
dc.creator.author | Rajalingam, Krishnaraj | |
cristin.unitcode | 185,15,29,40 | |
cristin.unitname | Seksjon for biokjemi og molekylærbiologi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.fulltext | postprint | |
cristin.qualitycode | 2 | |
dc.identifier.cristin | 1530358 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=EMBO Reports&rft.volume=18&rft.spage=733&rft.date=2017 | |
dc.identifier.jtitle | EMBO Reports | |
dc.identifier.volume | 18 | |
dc.identifier.issue | 5 | |
dc.identifier.startpage | 733 | |
dc.identifier.endpage | 744 | |
dc.identifier.doi | http://dx.doi.org/10.15252/embr.201643744 | |
dc.identifier.urn | URN:NBN:no-62348 | |
dc.type.document | Tidsskriftartikkel | en_US |
dc.type.peerreviewed | Peer reviewed | |
dc.source.issn | 1469-221X | |
dc.identifier.fulltext | Fulltext https://www.duo.uio.no/bitstream/handle/10852/59674/3/APi5-final.pdf | |
dc.type.version | AcceptedVersion | |