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- W83510051 abstract "Since the late 1980's, protein phosphorylation-mediatedmechanisms have been recognized as regulators of sorting and processing of the Alzheimer's amyloid precursor (APP). These phospho-state-sensitive steps, in turn, determine the quality and quantity of Aβ generation. Here, we review several recent advances in this field, including new evidence that: (1) the phospho-state of APP threonine-668 does not obviously regulate APP sorting, Aβ generation or Aβ speciation; (2) β-secretase (BACE) recycling is regulated by the phospho-state of the BACE cytoplasmic tail, but without impact on Aβ generation or speciation; (3) contrary to its well-documented acute actions, chronic protein kinase C activation increases Aβ generation; and (4) sorting of APP and/or its α- and β-carboxyl-terminal fragments (C83 and C99, respectively) toward the trans-Golgi network is under the influence of presenilins and the VPS35/retromer. With the recent discovery of genetic linkage between the risk for Alzheimer's disease (AD) and polymorphisms in SORL1, a gene belonging to the sortilin class of trafficking proteins, the membrane protein cell biology of APP has emerged as a central focus for investigators seeking to understand the basis of common forms of AD and thereby uncover new therapeutic opportunities for its treatment and/or prevention." @default.
- W83510051 created "2016-06-24" @default.
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- W83510051 date "2009-01-01" @default.
- W83510051 modified "2023-09-24" @default.
- W83510051 title "Amyloid Precursor Protein Sorting and Processing: Transmitters, Hormones, and Protein Phosphorylation Mechanisms" @default.
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- W83510051 doi "https://doi.org/10.1007/978-3-540-87941-1_1" @default.
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