Dysfunction of chaperone-mediated autophagy in human diseases.
Aging
Alzheimer Disease
/ metabolism
Amino Acid Motifs
Amyotrophic Lateral Sclerosis
/ metabolism
Animals
Autophagy
Chaperone-Mediated Autophagy
HSC70 Heat-Shock Proteins
/ metabolism
Homeostasis
Humans
Huntington Disease
/ metabolism
Hydrolysis
Lysosomal-Associated Membrane Protein 2
/ metabolism
Lysosomes
/ metabolism
Molecular Chaperones
/ metabolism
Neoplasms
/ metabolism
Neurodegenerative Diseases
Parkinson Disease
/ metabolism
Protein Processing, Post-Translational
T-Lymphocytes
/ metabolism
Cancer
Chaperone-mediated autophagy
KFERQ-like motif
Metabolic disorder
Neurodegenerative diseases
Journal
Molecular and cellular biochemistry
ISSN: 1573-4919
Titre abrégé: Mol Cell Biochem
Pays: Netherlands
ID NLM: 0364456
Informations de publication
Date de publication:
Mar 2021
Mar 2021
Historique:
received:
17
08
2020
accepted:
24
11
2020
pubmed:
4
1
2021
medline:
3
8
2021
entrez:
3
1
2021
Statut:
ppublish
Résumé
Chaperone-mediated autophagy (CMA), one of the degradation pathways of proteins, is highly selective to substrates that have KFERQ-like motif. In this process, the substrate proteins are first recognized by the chaperone protein, heat shock cognate protein 70 (Hsc70), then delivered to lysosomal membrane surface where the single-span lysosomal receptor, lysosome-associated membrane protein type 2A (LAMP2A) can bind to the substrate proteins to form a 700 kDa protein complex that allows them to translocate into the lysosome lumen to be degraded by the hydrolytic enzymes. This degradation pathway mediated by CMA plays an important role in regulating glucose and lipid metabolism, transcription, DNA reparation, cell cycle, cellular response to stress and consequently, regulating many aging-associated human diseases, such as neurodegeneration, cancer and metabolic disorders. In this review, we provide an overview of current research on the functional roles of CMA primarily from a perspective of understanding and treating human diseases and also discuss its potential applications for diseases.
Identifiants
pubmed: 33389491
doi: 10.1007/s11010-020-04006-z
pii: 10.1007/s11010-020-04006-z
doi:
Substances chimiques
HSC70 Heat-Shock Proteins
0
Lysosomal-Associated Membrane Protein 2
0
Molecular Chaperones
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1439-1454Subventions
Organisme : National Natural Science Foundation of China
ID : 81600470
Organisme : Qingdao Applied Basic Research Youth Project
ID : 19-6-2-59-cg
Organisme : China Postdoctoral Science Foundation Funded Project
ID : 2015M57074,2016T90612
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