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Beyond gamma-secretase activity: The multifunctional nature of presenilins in cell signalling pathways

机译：超越γ-分泌酶的活性：早老素在细胞信号通路中的多功能性质

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The presenilins are the catalytic subunit of the membrane-embedded tetrameric gamma-secretase protease complexes. More that 90 transmembrane proteins have been reported to be gamma-secretase substrates, including the widely studied amyloid precursor protein (APP) and the Notch receptor, which are precursors for the generation of amyloid-beta peptides and biologically active APP intracellular domain (AICD) and Notch intracellular domain (NICD). The diversity of gamma-secretase substrates highlights the importance of presenilin-dependent gamma-secretase protease activities as a regulatory mechanism in a range of biological systems. However, there is also a growing body of evidence that supports the existence of gamma-secretase-independent functions for the presenilins in the regulation and progression of an array of cell signalling pathways. In this review, we will present an overview of current literature that proposes evolutionarily conserved presenilin functions outside of the gamma-secretase complex, with a focus on the suggested role of the presenilins in the regulation of Wnt/beta-catenin signalling, protein trafficking and degradation, calcium homeostasis and apoptosis. (C) 2015 Elsevier Inc. All rights reserved.
机译：早老蛋白是膜包埋的四聚体γ-分泌酶蛋白酶复合物的催化亚基。据报道90多种跨膜蛋白是γ-分泌酶的底物，包括广泛研究的淀粉样前体蛋白（APP）和Notch受体，它们是淀粉样β肽和具有生物活性的APP细胞内结构域（AICD）生成的前体。和Notch细胞内结构域（NICD）。 γ-分泌酶底物的多样性突显了早老素依赖性γ-分泌酶蛋白酶活性在一系列生物系统中作为调节机制的重要性。但是，也有越来越多的证据支持早老素在一系列细胞信号通路的调控和进展中存在与γ-分泌酶无关的功能。在这篇综述中，我们将概述目前的文献，提出γ-分泌酶复合物以外的进化上保守的早老素功能，重点是早老素在调节Wnt /β-catenin信号传导，蛋白质转运和调节中的作用。降解，钙稳态和凋亡。 （C）2015 Elsevier Inc.保留所有权利。

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