Supporting data on prion protein translocation mechanism revealed by pulling force studies.

ABSTRACT: The Prion protein (PrP) is a highly conserved cell surface glycoprotein. To enter the secretory pathway, the PrP precursor relies on the Sec61 complex and multiple accessory factors all gathering at the membrane of the Endoplasmic reticulum (ER). PrP topogenesis results in the formation of different PrP isoforms. Aside from the typical secretory variant (^SecPrP) different pathognomonic, membrane-embedded variants (^NtmPrP and ^CtmPrP) that are associated with neurodegenerative diseases can be found [1]. In this article, we provide supportive data related to "Prion Protein Translocation Mechanism Revealed by Pulling Force Studies" (Kriegler et al., May 2020)[2], where we utilize Xbp1 arrest peptide (AP)-mediated ribosomal stalling to study the co-translational

SUBMITTER: Kriegler T 

PROVIDER: S-EPMC7334574 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature