Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1864, Issue 11, Pages 2128-2137Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2017.06.022
Keywords
Prion; Proteolysis; Shedding; ADAM10; Neurodegeneration; Neuropathology
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Funding
- Deutsche Forschungsgemeinschaft (Collaborative Research Center) [SFB877]
- Deutsche Forschungsgemeinschaft [GRK1459]
- Werner-Otto-Stiftung Hamburg
- Creutzfeldt-Jakob Disease Foundation, Inc.
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Proteolytic processing of the cellular and disease-associated form of the prion protein leads to generation of bioactive soluble prion protein fragments and modifies the structure and function of its cell-bound form. The nature of proteases responsible for shedding, alpha-, beta-, and gamma-cleavage of the prion protein are only partially identified and their regulation is largely unknown. Here, we provide an overview of the increasingly multifaceted picture of prion protein proteolysis and shed light on physiological and pathological roles associated with these cleavages. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.
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