Cargando…
Cytosolically expressed PrP GPI-signal peptide interacts with mitochondria
We previously reported that PrP GPI-anchor signal peptide (GPI-SP) is specifically degraded by the proteasome. Additionally, we showed that the point mutation P238S, responsible for a genetic form of prion diseases, while not affecting the GPI-anchoring process, results in the accumulation of PrP GP...
Autores principales: | Guizzunti, Gianni, Zurzolo, Chiara |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4594234/ https://www.ncbi.nlm.nih.gov/pubmed/26480298 http://dx.doi.org/10.1080/19420889.2015.1036206 |
Ejemplares similares
-
Detection of the GPI-anchorless prion protein fragment PrP226* in human brain
por: Dvorakova, Eva, et al.
Publicado: (2013) -
Heat shock protein 70 selectively mediates the degradation of cytosolic PrPs and restores the cytosolic PrP-induced cytotoxicity via a molecular interaction
por: Zhang, Jin, et al.
Publicado: (2012) -
GPI-anchor signal sequence influences PrP(C) sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice
por: Puig, Berta, et al.
Publicado: (2019) -
Damaged mitochondria and overproduction of ROS in Fanconi anemia cells
por: Lyakhovich, Alex
Publicado: (2013) -
Propagation of RML Prions in Mice Expressing PrP Devoid of GPI Anchor Leads to Formation of a Novel, Stable Prion Strain
por: Mahal, Sukhvir Paul, et al.
Publicado: (2012)