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早老素1:不仅仅是γ-分泌酶。

Presenilin 1: more than just gamma-secretase.

作者信息

Raemaekers T, Esselens C, Annaert W

机构信息

Laboratory for Membrane Trafficking, Center for Human Genetics, Gasthuisberg, K.U. Leuven and V.I.B.04, B-3000 Leuven, Belgium.

出版信息

Biochem Soc Trans. 2005 Aug;33(Pt 4):559-62. doi: 10.1042/BST0330559.

Abstract

Presenilin 1 plays a central catalytic role in the gamma-secretase processing of amyloid precursor protein, Notch and many other substrates. However, this core component clearly mediates independently several other physiological roles in the cell/neuron. Besides its involvement in beta-catenin degradation, we discuss here the recent implication of presenilin 1 in the turnover of the intercellular cell adhesion molecule, telencephalin, through a degradation route that bears autophagic characteristics. Activation of the endosomal/lysosomal system in general and autophagic degradation in particular, is finally briefly discussed in the context of neurodegenerative diseases.

摘要

早老素1在淀粉样前体蛋白、Notch及许多其他底物的γ-分泌酶加工过程中发挥核心催化作用。然而,这一核心成分显然在细胞/神经元中独立介导了其他几种生理作用。除了参与β-连环蛋白的降解外,我们在此讨论早老素1最近通过具有自噬特征的降解途径参与细胞间细胞黏附分子(脑端素)周转的情况。最后,在内神经退行性疾病的背景下简要讨论了一般内体/溶酶体系统的激活,特别是自噬降解。

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