APP and APLP1 are degraded through autophagy in response to proteasome inhibition in neuronal cells

Zhou, Fangfang; van Laar, Theo; Huang, Huizhe; Zhang, Long

doi:10.1007/s13238-011-1047-9

Cited by 63Alzheimer's disease research and treatmentsAutophagy in Disease and TherapyUbiquitin and proteasome pathways

APP and APLP1 are degraded through autophagy in response to proteasome inhibition in neuronal cells

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Zhou, Fangfang, van Laar, Theo, Huang, Huizhe, Zhang, Long·2011·Protein & Cell

DOI 10.1007/s13238-011-1047-9PMC PMC4875337

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Abstract

Amyloid beta (Aβ) precursor protein (APP) is a key protein in the pathogenesis of Alzheimer's disease (AD). Both APP and its paralogue APLP1 (amyloid beta precursor-like protein 1) have multiple functions in cell adhesion and proliferation. Previously it was thought that autophagy is a novel beta-amyloid peptide (Aβ)-generating pathway activated in AD. However, the protein proteolysis of APLP1 is still largely unknown. The present study shows that APLP1 is rapidly degraded in neuronal cells in response to stresses, such as proteasome inhibition. Activation of the endoplasmic reticulum (ER) stress by proteasome inhibitors induces autophagy, causing reduction of mature APLP1/APP. Blocking autophagy or JNK stress kinase rescues the protein expression for both APP and APLP1. Therefore, our results suggest that APP/APLP1 is degraded through autophagy and the APLP1 proteolysis is mainly mediated by autophagy-lysosome pathway.

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Autophagy facilitates Amyloid Precursor Protein (APP) degradation and Aβ clearance.
“Since autophagy facilitates Amyloid Precursor Protein (APP) degra dation and A β clearance (Son et al., 2012; Zhou et al., 2011)”
From Nilotinib restores memory function by preventing dopaminergic neuron degeneration in a mouse model of Alzheimer’s Disease (2021) · cites this paper as Zhou et al., 2011

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Authors: Zhou, F., van Laar, T., Huang, H., & Zhang, L.
Affiliations: Leiden University Medical Center (NL)
Chongqing Medical University (CN)
Corresponding author: Huang, Huizhe
Zhang, Long
ORCID: Zhou, Fangfang
Huang, Huizhe
Zhang, Long
Venue: Protein & Cell
Publisher: Oxford University Press (OUP)
Published: 2011-05
Volume: 2
Issue: 5
Pages: 377-383
ISSN: 1674-800X (ISSN-L)
1674-8018
DOI: 10.1007/s13238-011-1047-9
PMC: PMC4875337
OpenAlex: W1964677366
Cited by: 63
References: 23
Citations by year: 2025: 3 · 2024: 6 · 2023: 2 · 2022: 6 · 2021: 6 · 2020: 8 · 2019: 7 · 2017: 4 · 2016: 3 · 2015: 4 · 2013: 5 · 2012: 8
FWCI: 2.84
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Protein & Cell (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Leiden Repository (Leiden University) (submittedVersion)
Funders: National Natural Science Foundation of China
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: amyloid precursor protein, APLP1, autophagy, proteasome inhibition, protein degradation, endoplasmic reticulum stress, autophagy-lysosome pathway, Alzheimer's disease, neurons, proteolysis
MeSH terms: Animals, Autophagy, Cell Line, Endoplasmic Reticulum, Leupeptins, Neurons, Amyloid beta-Protein Precursor, Proteasome Endopeptidase Complex, JNK Mitogen-Activated Protein Kinases, Mice, Rats, Protein Stability, Proteasome Inhibitors

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APP and APLP1 are degraded through autophagy in response to proteasome inhibition in neuronal cells

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