Mechanisms of Selective Autophagy
Open accessAbstract
Selective autophagy is the lysosomal degradation of specific intracellular components sequestered into autophagosomes, late endosomes, or lysosomes through the activity of selective autophagy receptors (SARs). SARs interact with autophagy-related (ATG)8 family proteins via sequence motifs called LC3-interacting region (LIR) motifs in vertebrates and Atg8-interacting motifs (AIMs) in yeast and plants. SARs can be divided into two broad groups: soluble or membrane bound. Cargo or substrate selection may be independent or dependent of ubiquitin labeling of the cargo. In this review, we discuss mechanisms of mammalian selective autophagy with a focus on the unifying principles employed in substrate recognition, interaction with the forming autophagosome via LIR-ATG8 interactions, and the recruitment of core autophagy components for efficient autophagosome formation on the substrate.
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Ubiquitin-independent mitophagy mainly depends on outer mitochondrial membrane-resident mitophagy receptors including BNIP3L/NIX, FUNDC1, and FKBP8 in mammals.
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Kriegenburg, F., Ungermann, C., & Reggiori, F. (2018) · Current Biology · doi:10.1016/j.cub.2018.02.034 · Cited by 95 · see citing works
Atg8-Family Proteins—Structural Features and Molecular Interactions in Autophagy and Beyond
Wesch, N., Kirkin, V., & Rogov, V. V. (2020) · Cells · doi:10.3390/cells9092008 · Cited by 93 · see citing works
Abreu, S., Kriegenburg, F., Gómez‐Sánchez, R., Mari, M. C., Sánchez, J., Rasmussen, M. S., Guimarães, R. S., Zens, B., Schuschnig, M., Hardenberg, R., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643146 · Cited by 85 · see citing works
Self-citationPotent and specific Atg8-targeting autophagy inhibitory peptides from giant ankyrins
Li, J., Zhu, R., Chen, K., Zheng, H., Zhao, H., Yuan, C., Zhang, H., Wang, C., & Zhang, M. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0082-8 · Cited by 83 · see citing works
A UPR-Induced Soluble ER-Phagy Receptor Acts with VAPs to Confer ER Stress Resistance
Zhao, D., Zou, C., Liu, X., Jiang, Z., Zhong-qiu, Y., Suo, F., Du, T.-Y., Dong, M., He, W., & Du, L. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.019 · Cited by 78 · see citing works
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TRIM17 contributes to autophagy of midbodies while actively sparing other targets from degradation
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Autophagy and the hallmarks of aging
Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285 · see citing works
Exerkines and Sarcopenia: Unveiling the Mechanism Behind Exercise-Induced Mitochondrial Homeostasis
Wang, J., Jia, D., Zhang, Z., & Wang, D. (2025) · Metabolites · doi:10.3390/metabo15010059 · Cited by 23 · see citing works
Targeted protein modification as a paradigm shift in drug discovery
Amirian, R., Azadi Badrbani, M., Izadi, Z., Samadian, H., Bahrami, G., Sarvari, S., Abdolmaleki, S., Nabavi, S. M., Derakhshankhah, H., & Jaymand, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115765 · Cited by 18 · see citing works
AlphaFold2 SLiM screen for LC3-LIR interactions in autophagy
Stuke, J. F. M., & Hummer, G. (2025) · Autophagy · doi:10.1080/15548627.2025.2493999 · Cited by 8 · see citing works
Cuní-López, C., Root, J. T., Hao, Y., Blomberg, N., Koppes-den Hertog, S. J., Sacks, D., Trujillo, A. E., Ghirlando, R., Kowal, I., Epstein, J., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76565-6
- Authors
- Lamark, T., & Johansen, T.
- Affiliations
- UiT The Arctic University of Norway (NO)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2021-10-06
- Volume
- 37
- Issue
- 1
- Pages
- 143-169
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W3176556289
- Cited by
- 429
- References
- 183
- Citations by year
- 2026: 81 · 2025: 112 · 2024: 110 · 2023: 74 · 2022: 41 · 2021: 11
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- other-oa
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- NORA - Norwegian Open Research Archives (submittedVersion, other-oa)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- selective autophagy, autophagy receptors, LC3-interacting region, Atg8-family proteins, autophagosome formation, substrate recognition, cargo selection, lysosomal degradation
- MeSH terms
- Autophagosomes, Autophagy-Related Protein 8 Family, Animals, Autophagy, Mammals, Microtubule-Associated Proteins, Apoptosis Regulatory Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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