磷酸化状态依赖的Aβ神经内分选不同地损害自噬和内溶酶体系统。

IF 14.6 1区生物学 Q1 CELL BIOLOGY

Autophagy Pub Date : 2024-01-01 Epub Date: 2023-08-29 DOI:10.1080/15548627.2023.2252300

Akshay Kapadia, Sandra Theil, Sabine Opitz, Nàdia Villacampa, Hannes Beckert, Susanne Schoch, Michael T Heneka, Sathish Kumar, Jochen Walter

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引用次数: 0

摘要

缩写：AD：阿尔茨海默病；APP：淀粉样蛋白β前体蛋白；ATG：自噬相关；Aβ：淀粉样蛋白-β；CTSD：组织蛋白酶D；DAPI:4’，6-二脒基-2-苯基吲哚；EEA1：早期内体抗原1；FA：甲酸；GFP：绿色荧光蛋白；LAMP2：溶酶体相关膜蛋白2；MAP1LC3/LC3：微管相关蛋白1轻链3；MAP2：微管相关蛋白2；nmAβ：非修饰淀粉样蛋白-β；npAβ：非磷酸化淀粉样蛋白-β；pAβ：磷酸化淀粉样蛋白-β；p-Ser26Aβ：丝氨酸残基26处磷酸化的淀粉样蛋白-β；p-Ser8Aβ：丝氨酸残基8磷酸化的淀粉样蛋白-β；RAB:RAB，RAS癌基因家族成员；RFP：红色荧光蛋白；SQSTM1/p62：螯合体1；YFP：黄色荧光蛋白。

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Phosphorylation-state dependent intraneuronal sorting of Aβ differentially impairs autophagy and the endo-lysosomal system.

Abbreviations: AD: Alzheimer disease; APP: amyloid beta precursor protein; ATG: autophagy related; Aβ: amyloid-β; CTSD: cathepsin D; DAPI: 4',6-diamidino-2-phenylindole; EEA1: early endosome antigen 1; FA: formic acid; GFP: green fluorescent protein; LAMP2: lysosomal-associated membrane protein 2; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MAP2: microtubule-associated protein 2; nmAβ: non-modified amyloid-β; npAβ: non-phosphorylated amyloid-β; pAβ: phosphorylated amyloid-β; p-Ser26Aβ: amyloid-β phosphorylated at serine residue 26; p-Ser8Aβ: amyloid-β phosphorylated at serine residue 8; RAB: RAB, member RAS oncogene family; RFP: red fluorescent protein; SQSTM1/p62: sequestome 1; YFP: yellow fluorescent protein.

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来源期刊

Autophagy 生物-细胞生物学

CiteScore

21.30

自引率

2.30%

发文量

277

审稿时长

1 months

期刊介绍： Autophagy is a peer-reviewed journal that publishes research on autophagic processes, including the lysosome/vacuole dependent degradation of intracellular material. It aims to be the premier journal in the field and covers various connections between autophagy and human health and disease, such as cancer, neurodegeneration, aging, diabetes, myopathies, and heart disease. Autophagy is interested in all experimental systems, from yeast to human. Suggestions for specialized topics are welcome. The journal accepts the following types of articles: Original research, Reviews, Technical papers, Brief Reports, Addenda, Letters to the Editor, Commentaries and Views, and Articles on science and art. Autophagy is abstracted/indexed in Adis International Ltd (Reactions Weekly), EBSCOhost (Biological Abstracts), Elsevier BV (EMBASE and Scopus), PubMed, Biological Abstracts, Science Citation Index Expanded, Web of Science, and MEDLINE.