NUFIP1 is a ribosome receptor for starvation-induced ribophagy
Open accessAbstract
The lysosome degrades and recycles macromolecules, signals to the master growth regulator mTORC1 [mechanistic target of rapamycin (mTOR) complex 1], and is associated with human disease. We performed quantitative proteomic analyses of rapidly isolated lysosomes and found that nutrient levels and mTOR dynamically modulate the lysosomal proteome. Upon mTORC1 inhibition, NUFIP1 (nuclear fragile X mental retardation-interacting protein 1) redistributes from the nucleus to autophagosomes and lysosomes. Upon these conditions, NUFIP1 interacts with ribosomes and delivers them to autophagosomes by directly binding to microtubule-associated proteins 1A/1B light chain 3B (LC3B). The starvation-induced degradation of ribosomes via autophagy (ribophagy) depends on the capacity of NUFIP1 to bind LC3B and promotes cell survival. We propose that NUFIP1 is a receptor for the selective autophagy of ribosomes.
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Defective ribosomal components may be removed through ribophagy, a selective form of autophagy targeting ribosomes.
“Defective ribosomal components may subsequently be removed through ribophagy, a selective form of autophagy targeting ribosomes [64].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [64]
The Abstract (page unavailable) describes ribophagy as selective autophagy of ribosomes, supporting the mechanism in the claim. The section on nutrient-starvation-induced ribosomal degradation (page unavailable) studies degradation of ribosomes during starvation, not the removal of defective ribosomal components; it separately says unassembled ribosomal proteins are degraded by the proteasome. (LLM, conf=0.87)
Experimental — accuracy not yet measuredRibosome degradation is mediated in part by ribophagy, a selective form of autophagy.
“Ribosome degradation is mediated in part by ribophagy, a selective form of autophagy”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [64]
Mature mammalian ribosomes are exceptionally stable, with estimated in vivo half-lives spanning several days to over a week, so total RNA accumulation lags behind immediate Pol I activation.
“As mature mammalian ribosomes are exceptionally stable, with estimated in vivo half-lives spanning several days to over a week [25,64], total RNA accumulation lags significantly behind the immediate activation of RNA polymerase I [34].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [64]
The Conclusions (page unavailable) discuss starvation-induced ribosome degradation and the fraction of cellular RNA in ribosomes, but give no in vivo ribosome half-lives. Searches for “half-life” and ribosome stability found no passage supporting the estimate of several days to over a week. The separate claim about Pol I activation is attached to a different citation. (LLM, conf=0.72)
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- Authors
- Wyant, G. A., Abu-Remaileh, M., Frenkel, E. M., Laqtom, N. N., Dharamdasani, V., Lewis, C. A., Chan, S. H., Heinze, I., Ori, A., & Sabatini, D. M.
- Affiliations
- Broad Institute (US)
- Whitehead Institute for Biomedical Research (US)
- Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) (DE)
- Leibniz Institute on Aging–Fritz Lipmann Institute, 07745 Jena, Germany.
- Corresponding author
- Wyant, Gregory A.
- Abu-Remaileh, Monther
- Sabatini, David M.
- ORCID
- Venue
- Science
- Published
- 2018-05-18
- Volume
- 360
- Issue
- 6390
- Pages
- 751-758
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC6020066
- OpenAlex
- W2802593879
- Cited by
- 363
- References
- 52
- Citations by year
- 2026: 27 · 2025: 40 · 2024: 46 · 2023: 32 · 2022: 44 · 2021: 56 · 2020: 58 · 2019: 43 · 2018: 17
- FWCI
- 34.33
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc)
- PMC
- Funders
- U.S. Department of Defense (W81XWH-15-1-0230)
- NIH Office of the Director (R01 CA103866, R01 CA129105, R37 AI47389)
- Glenn Foundation for Medical Research (Postdoctoral Fellowship for Translational Research on Aging)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- ribophagy, selective autophagy, ribosome degradation, starvation, mTORC1, LC3B, autophagosomes, nutrient signaling, cell survival
- MeSH terms
- Autophagosomes, Amino Acids, Animals, Autophagy, Cell Nucleus, Humans, Lysosomes, Microtubule-Associated Proteins, Nuclear Proteins, Ribosomes, Transcription Factors, RNA-Binding Proteins, Receptors, Cytoplasmic and Nuclear, Proteome, Proteomics, Mice, HEK293 Cells, TOR Serine-Threonine Kinases
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