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The ability of PrP\n                    <jats:sup>C<\/jats:sup>\n                    to serve as a substrate for this template\u2010mediated conversion process depends on several criteria but importantly includes the presence or absence of certain endoproteolytic events performed at the cell surface or in acidic endolysosomal compartments. The major endoproteolytic events affecting PrP\n                    <jats:sup>C<\/jats:sup>\n                    are referred to as \u03b1\u2010 and \u03b2\u2010cleavages, and in this review we outline the sites within PrP\n                    <jats:sup>C<\/jats:sup>\n                    at which the cleavages occur, the mechanisms potentially responsible and their relevance to pathology. Although the association of \u03b1\u2010cleavage with neuroprotection is well\u2010supported, we identify open questions regarding the importance of \u03b2\u2010cleavage in TSEs and suggest experimental approaches that could provide clarification. We also combine findings from in\u00a0vitro cleavage assays and mass spectrometry\u2010based studies of prion protein fragments in the brain to present an updated view in which \u03b1\u2010 and \u03b2\u2010cleavages may represent two distinct clusters of proteolytic events that occur at multiple neighbouring sites rather than at single positions. Furthermore, we highlight the candidate proteolytic mechanisms best supported by the literature; currently, despite several proteases identified as capable of processing PrP\n                    <jats:sup>C<\/jats:sup>\n                    in\u00a0vitro, in cell\u2010based models and in some cases, in\u00a0vivo, none have been shown conclusively to cleave PrP\n                    <jats:sup>C<\/jats:sup>\n                    in the brain. Addressing this knowledge gap will be crucial for developing therapeutic interventions to drive PrP\n                    <jats:sup>C<\/jats:sup>\n                    endoproteolysis in a neuroprotective direction. Finally, we end this review by briefly addressing other cleavage events, specifically ectodomain shedding, \u03b3\u2010cleavage, the generation of atypical pathological fragments in the familial prion disorder Gerstmann\u2013Str\u00e4ussler\u2013Scheinker syndrome and the possibility of an additional form of endoproteolysis close to the PrP\n                    <jats:sup>C<\/jats:sup>\n                    N\u2010terminus.\n                    <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                      <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc16310-fig-0005-m.png\">\n                        <jats:alt-text>image<\/jats:alt-text>\n                      <\/jats:graphic>\n                    <\/jats:boxed-text>\n                  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