Proteasomal Inhibition Redirects the PrP-Like Shadoo Protein to the Nucleus.

ABSTRACT: The Shadoo protein (Sho) exhibits homology to the hydrophobic region of the cellular isoform of prion protein (PrP^C). As prion-infected brains gradually accumulate infectivity-associated isoforms of prion protein (PrP^Sc), levels of mature endogenous Sho become reduced. To study the regulatory effect of the proteostatic network on Sho expression, we investigated the action of lactacystin, MG132, NH₄Cl, and 3-methyladenine (3-MA) in two cell culture models. In primary mixed neuronal and glial cell cultures (MNGCs) from transgenic mice expressing wild-type Sho from the PrP gene promoter (Tg.Sprn mice), lactacystin- and MG132-mediated inhibition of proteasomal activity shifted the repertoire of Sho species towards unglycosylated forms appearing in the nuclei; c

SUBMITTER: Kang SG 

PROVIDER: S-EPMC6815274 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature