title: The HET-S/s Prion Motif in the Control of Programmed Cell Death.
abstract: The [Het-s] prion of the fungus Podospora anserina is a well-studied model system to elucidate the action of prions and beyond. The [Het-s] prion works as an activation trigger of a cell death execution protein termed HET-S. Amyloid transconformation of the prion-forming region of HET-S induces activation of its pore-forming cell death execution HeLo domain. The prion motif functions in a signal transduction process by which a nucleotide-binding oligomerization domain (NOD)-like receptor termed NWD2 controls the HET-S cell death effector. This prion motif thus corresponds to a functional amyloid motif, allowing a conformational crosstalk between homologous motif domains in signal transduction processes that appears to be widespread from the fungal to the mammalian animal kingdoms. This review aims to establish a structure-activity relationship of the HET-S/s prion system and sets it in the context of its wider biological significance.
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, 8093 Zürich, Switzerland.
authors.forename: Roland
authors.initials: R
authors.lastname: Riek
authors.affiliation: Institut de Biochimie et de Génétique Cellulaire UMR 5095, CNRS - Université de Bordeaux, 33077 Bordeaux, France.
authors.forename: Sven J
authors.initials: SJ
authors.lastname: Saupe
mesh_terms: D017209:Apoptosis; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D048468:Podospora / Q000378:metabolism*; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D013329:Structure-Activity Relationship
chemical_list: D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D011328:Prions