• Robert J Andrew, Katherine A B Kellett, Gopal Thinakaran, and Nigel M Hooper.
• From the Departments of Neurobiology, Neurology, and Pathology, The University of Chicago, Chicago, Illinois 60637 and rjandrew@uchicago.edu.
• J. Biol. Chem. 2016 Sep 9; 291 (37): 19235-44.

AbstractProteolysis of the amyloid precursor protein (APP) liberates various fragments including the proposed initiator of Alzheimer disease-associated dysfunctions, amyloid-β. However, recent evidence suggests that the accepted view of APP proteolysis by the canonical α-, β-, and γ-secretases is simplistic, with the discovery of a number of novel APP secretases (including δ- and η-secretases, alternative β-secretases) and additional metabolites, some of which may also cause synaptic dysfunction. Furthermore, various proteins have been identified that interact with APP and modulate its cleavage by the secretases. Here, we give an overview of the increasingly complex picture of APP proteolysis.© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

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