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Cited by 111Autophagy in Disease and TherapyHeat shock proteins researchUbiquitin and proteasome pathways

Chaperone‐mediated autophagy: Molecular mechanisms, biological functions, and diseases

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Yao, Ruchen, Shen, Jun·2023·MedComm
DOI 10.1002/mco2.347PMC PMC10466100
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Abstract

Chaperone‐mediated autophagy (CMA) is a lysosomal degradation pathway that eliminates substrate proteins through heat‐shock cognate protein 70 recognition and lysosome‐associated membrane protein type 2A‐assisted translocation. It is distinct from macroautophagy and microautophagy. In recent years, the regulatory mechanisms of CMA have been gradually enriched, including the newly discovered NRF2 and p38–TFEB signaling, as positive and negative regulatory pathways of CMA, respectively. Normal CMA activity is involved in the regulation of metabolism, aging, immunity, cell cycle, and other physiological processes, while CMA dysfunction may be involved in the occurrence of neurodegenerative disorders, tumors, intestinal disorders, atherosclerosis, and so on, which provides potential targets for the treatment and prediction of related diseases. This article describes the general process of CMA and its role in physiological activities and summarizes the connection between CMA and macroautophagy. In addition, human diseases that concern the dysfunction or protective role of CMA are discussed. Our review deepens the understanding of the mechanisms and physiological functions of CMA and provides a summary of past CMA research and a vision of future directions.

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  • Macroautophagy is a multistep process regulated by mTORC1 and ULK1 signaling that culminates in formation of double-membraned autophagosomes, which fuse with lysosomes to form autolysosomes.

    “and (iii) macroautophagy (commonly referred to simply as autophagy), a multistep process regulated by mammalian target of rapamycin 1 (mTORC1) and Unc-51 like autophagy activating kinase 1 (ULK1) signaling that culminates in the formation of double-membraned autophagosomes, which fuse with lysosomes to form autolysosomes [133–135].”

    From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [134]

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Cited by

Sorted by citations

Authors
Yao, R., & Shen, J.
Affiliations
Shanghai Jiao Tong University (CN)
Corresponding author
Shen, Jun
ORCID
Shen, Jun
Venue
MedComm
Publisher
Wiley
Published
2023-08-30
Volume
4
Issue
5
Pages
e347-e347
ISSN
2688-2663 (ISSN-L)
DOI
10.1002/mco2.347
PMC
PMC10466100
OpenAlex
W4386292310
Cited by
111
References
20
Citations by year
2026: 45 · 2025: 48 · 2024: 18
FWCI
4.08
Type
journal article
Language
en
Open access
Licence
Locations
  • MedComm (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Shanghai Jiao Tong University (RJPY‐LX‐004)
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
chaperone-mediated autophagy, Hsc70, LAMP2A, lysosomal degradation, Nrf2 signaling, macroautophagy, aging, neurodegenerative diseases, tumors, intestinal disorders, atherosclerosis

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