Show simple item record

Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis

dc.contributor.authorDASKALOV, Asen
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorSABATE, Raimon
dc.contributor.authorBERBON, Melanie
dc.contributor.authorMARTINEZ, Denis
dc.contributor.authorCHAIGNEPAIN, Stephane
dc.contributor.authorCOULARY-SALIN, Benedicte
dc.contributor.authorHOFMANN, Kay
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorSAUPE, Sven J.
dc.date.accessioned2020-09-03T07:56:22Z
dc.date.available2020-09-03T07:56:22Z
dc.date.issued2016
dc.identifier.issn0027-8424
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10885
dc.description.abstractEnRecent findings have revealed the role of prion-like mechanisms in the control of host defense and programmed cell death cascades. In fungi, HET-S, a cell death-inducing protein containing a HeLo pore-forming domain, is activated through amyloid templating by a Nod-like receptor (NLR). Here we characterize the HELLP protein behaving analogously to HET-S and bearing a new type of N-terminal cell death-inducing domain termed HeLo-like (HELL) and a C-terminal regulatory amyloid motif known as PP. The gene encoding HELLP is part of a three-gene cluster also encoding a lipase (SBP) and a Nod-like receptor, both of which display the PP motif. The PP motif is similar to the RHIM amyloid motif directing formation of the RIP1/RIP3 necrosome in humans. The C-terminal region of HELLP, HELLP(215-278), encompassing the motif, allows prion propagation and assembles into amyloid fibrils, as demonstrated by X-ray diffraction and FTIR analyses. Solid-state NMR studies reveal a well-ordered local structure of the amyloid core residues and a primary sequence that is almost entirely arranged in a rigid conformation, and confirm a beta-sheet structure in an assigned stretch of three amino acids. HELLP is activated by amyloid templating and displays membrane-targeting and cell death-inducing activity. HELLP targets the SBP lipase to the membrane, suggesting a synergy between HELLP and SBP in membrane dismantling. Remarkably, the HeLo-like domain of HELLP is homologous to the pore-forming domain of MLKL, the cell death-execution protein in necroptosis, revealing a transkingdom evolutionary relationship between amyloid-controlled fungal programmed cell death and mammalian necroptosis.
dc.language.isoen
dc.title.enIdentification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis
dc.typeArticle de revue
dc.identifier.doi10.1073/pnas.1522361113
dc.subject.halChimie/Matériaux
bordeaux.journalProceedings of the National Academy of Sciences of the United States of America
bordeaux.page2720-2725
bordeaux.volume113
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue10
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America&rft.date=2016&rft.volume=113&rft.issue=10&rft.spage=2720-2725&rft.epage=2720-2725&rft.eissn=0027-8424&rft.issn=0027-8424&rft.au=DASKALOV,%20Asen&HABENSTEIN,%20Birgit&SABATE,%20Raimon&BERBON,%20Melanie&MARTINEZ,%20Denis&rft.genre=article


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record