Abstract
Ribophagy is a selective autophagic process that regulates ribosome turnover. Although NUFIP1 has been identified as a mammalian receptor for ribophagy, its homologues do not exist in yeast and nematodes. Here we demonstrate that Rpl12, a ribosomal large subunit protein, functions as a conserved ribophagy receptor in multiple organisms. Disruption of Rpl12–Atg8s binding leads to significant accumulation of ribosomal proteins and rRNA, while Atg1-mediated Rpl12 phosphorylation enhances its association with Atg11, thus triggering ribophagy during starvation. Ribophagy deficiency accelerates cell death induced by starvation and pathogen infection, leading to impaired growth and development and a shortened lifespan in both Caenorhabditis elegans and Drosophila melanogaster. Moreover, ribophagy deficiency results in motor impairments associated with ageing, while the overexpression of RPL12 significantly improves movement defects induced by starvation, ageing and Aβ accumulation in fly models. Our findings suggest that Rpl12 functions as a conserved ribophagy receptor vital for ribosome metabolism and cellular homeostasis.
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Data availability
The MS proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE repository55,56 (ftp://massive.ucsd.edu/v08/MSV000096540/ and ftp://massive.ucsd.edu/v08/MSV000096542/), with the dataset identifier MassIVE MSV000096540 (or PXD058305) and MSV000096542 (or PXD058307). The raw LC–MS-based untargeted metabolomics data files generated in this study are available at the National Genomics Data Center57 (https://ngdc.cncb.ac.cn/omix/releaseList) with the dataset identifier OMIX008012 (https://ngdc.cncb.ac.cn/omix/release/OMIX008012) and are publicly available. Source data are provided with this paper. All of the other data supporting the findings of this study are available from the corresponding author upon reasonable request.
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Acknowledgements
We are grateful to Y. Ohsumi, H. Nakatogawa and Z. Xie for generously providing the plasmids and yeast strains. We also thank L. Yu, N. Gao, D. Pan, Y. Zhen and all other lab members for their insightful reading and constructive discussions on the paper. A special thanks to the technical support of Y. Zhang from cryo-electron microscopy core facilities, Zhejiang University School of Medicine; J. Zhou, F. He, C. Ma, Y. Wu and M. Xue for their assistance with the polysome profiling assay; Z. Wu for his guidance on mouse euthanasia and tissue protein extraction; D. Fang and H. Fan for their analysis and processing of metabolomics data from mouse liver; D. Neculai and S. Yan for providing Salmonella typhimurium carrying the RFP marker; and H. Zhang for providing the C. elegans cup-5(bp510) mutant. The research was supported by National Natural Science Foundation of China (grant nos. 32122028, 92254307 and 32070739) and Zhejiang Provincial Natural Science Foundation of China under grant no. LR21C070001 to C.Y.; the Research Funds of Hangzhou Institute for Advanced Study, UCAS (grant no. 2022ZZ01011) to Y.H.; National Natural Science Foundation of China (grant no. 32100600) to W.Y.; National Natural Science Foundation of China (grant nos. 32370822 and 31970919) to W.Z.; and the National Key Research and Development Program of China (grant no. 2021YFC2600104) to L.Z.
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Y.C., K.M., W.Z., Y.H., D.F. and C.Y. performed experiments, analysed data and wrote the paper. J.H., P.Z., J.F., Y.K., Z.L., S.D., W.Y., Y.D., X.W., Y.P., J.W., J.Y., M.F., K.T., X.L. and Y.Z. performed experiments and analysed data. J.Z., Z.X., H.X., C.W., L.Z., S.F., Z.H., Z.Y., W.L., Q.S. and B.Y. analysed data. All authors approved the final version of the paper.
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Extended data
Extended Data Fig. 1 Identifying the binding region(s) on Rpl12 associated with Atg8 and Atg11 in yeast.
a, Protein samples from Fig. 1b were separated by SDS-PAGE and analyzed by mass spectrometry (MS). The indicated ribosomal proteins binds to Atg8 but does not bind to the Atg8Y49A-L50A mutant. b, The AH109 strain was transformed with the indicated proteins fused with Atg8-BD, then grown on the indicated agar plates at 30 °C for 3 d. c, Schematic representation of the Atg11 domains. d, atg11∆ yeast cells co-expressing either WT HA-Atg11 or HA-Atg11 variants with Rpl12-GFP were subjected to SD-N for 1 h. Cell lysates were immunoprecipitated using anti-GFP agarose beads and analyzed by western blot with anti-HA antibody. e, Ni-NTA pulldowns were performed using purified His-TF-Rpl12 protein with GST-Atg11 R1, R2, R3, or CC4 proteins from E. Coli. f, The AH109 strain was transformed with either Rpl12 or the indicated Rpl12 variants fused with AD and Atg8-BD, then grown on the indicated agar plates at 30 °C for 3 d. g, Schematic representation of the Rpl12 domains and mutations, including N-terminal domain (NTD) and C-terminal domain (CTD). h-m, The AH109 strain was transformed with either Rpl12 or the indicated Rpl12 variants fused with AD and Atg8-BD, and subsequently grown on the indicated agar plates at 30 °C for 3 d. n, Tandem mass spectra of cross-linked peptide (AVGGEVGASAALAPKIGPLGLSPK-AEKSDIPEIDKR) demonstrate a direct interaction between Rpl12 and Atg8, with the Rpl12 E21 site is close to Atg8Y49-L50 sites. o, Western blot analysis shows that Rpl12 K4FSY cross-linked with Atg8 in vitro. Blots, gels, and Y2H assays are representatives of three independent experiments. Unprocessed blots/gels are available in Source data.
Extended Data Fig. 2 Rpl12 is required for starvation-induced ribophagy in yeast.
a, The indicated cells were grown on YPD with or without IAA agar plate at 30 °C for 2 days. b, rpl12b∆ or rpl12b∆ pep4∆ yeast cells expressing Rpl12a-mini-AID-3×FLAG were subjected to SD-N for the indicated times. Protein levels were analyzed by Western blot using anti-FLAG antibody. c, The ratio of Rpl12a-mini-AID-3×FLAG degradation was quantified from (b). d-k, The indicated yeast cells expressing GFP-tagged ribosomal proteins were treated with IAA for 2 h and subjected to SD-N for 0 or 6 h. Ribophagic activity were analyzed by western blot for the cleavage of GFP fusion protein. l, The indicated yeast cells were treated with IAA for 2 h and subjected to SD-N for 0 or 12 h. Ribosomal protein levels were analyzed by Western blot. m, Degradation ratios of proteins in (l) were quantified. n, Total RNA was extracted from the indicated yeast cells treated with IAA and subjected to SD-N for 0 or 6 h to assess rRNA levels. o, Yeast rRNA from (n) were quantified. p, q, rpl34a∆ or rps9a∆ cells expressing Rpl34b-mini-AID-3× FLAG (Rpl34b-AID) or Rps9b-mini-AID-3× FLAG (Rps9b-AID) were subjected to 0.5 mM IAA treatment for 0 or 2 h, Rps9a/Rpl34b-AID expression was detected by anti-FLAG antibody. The data are representatives of two independent experiments. r, The indicated yeast cells expressing GFP-tagged ribosomal proteins were treated with IAA for 2 h, and then subjected to SD-N for 0 or 6 h. Ribophagic activity were analyzed by western blot for the cleavage of GFP fusion protein. The results were quantified (see Methods). s, Total RNA of the indicated yeast cells was extracted to assess rRNA levels. t, Yeast rRNAs from (s) were quantified. Pgk1 served as a loading control. Blots, gels, and Y2H assays are representatives of three independent experiments unless specified in the legends. ***P < 0.001, ns, no significance. P values were calculated by two-tailed Student’s t tests (c, m, o, t) and data are presented as mean ± s.d. (n = 3 biological replicates). Exact P values, source numerical data and unprocessed blots/gels are available in Source data.
Extended Data Fig. 3 Vacuole is required for the degradation of ribosomal proteins and rRNAs under starvation conditions.
a, The indicated yeast cells were subjected to SD-N for the indicated times and protein levels were analyzed by western blot. b, Degradation ratios of proteins in (a) were quantified. c, WT, pep4∆, or atg1∆ yeast cells were grown to mid-log phase, pretreated with 100 µg/ml cycloheximide (CHX) for 1 h, and subsequently treated with 0.2 µg/ml rapamycin for 0, 2, 4, and 6 h. Ribosomal proteins were analyzed by Western blot. d, Degradation ratios of proteins in (c) were quantified. e, BY4741, rny1∆, or atg1∆ yeast cells were subjected to SD-N for 0, 2, 4, or 6 h. Total RNA was extracted from 5OD yeast cells to assess rRNA levels. f, Yeast rRNA from (e) was quantified. g, The indicated yeast cells were treated with IAA for 2 h and then subjected to SD-N for 0 or 6 h. Total RNA was extracted from 5OD yeast cells to assess rRNA levels. h, The rRNA levels from (g) were quantified. i, The indicated yeast cells were treated with IAA for 2 h and then subjected to SD-N for 0 or 6 h. A total of 5 OD600 yeast cells were harvested, and total RNA was extracted to assess yeast rRNA levels. j, The rRNA levels from panels (i) were quantified. k-n, The indicated yeast cells expressing the indicated ribosomal proteins fused with GFP tags were treated with IAA for 2 h, and then subjected to SD-N for 0 or 6 h. Ribophagic activity were analyzed by western blot to detect cleavage of GFP-fusion protein. Pgk1 served as a loading control. Blots and gels are representatives of three independent experiments. Statistical significance: ***P < 0.001, ns, no significance. P values were calculated by two-tailed Student’s t tests (b, d, f, h, j) and the data are presented as mean ± SD (n = 3 biological replicates). Exact P values, source numerical data and unprocessed blots/gels are provided in Source data.
Extended Data Fig. 4 Rpl12 is a substrate for Atg1 and the identification of phosphorylation sites on Rpl12 by Atg1.
a, In vitro kinase assays were performed using purified His-TF-Rpl12 from E. coli as substrates, with purified HA-Tor1 or HA-Tor1 KD (kinase dead) from yeast cells serving as protein kinase. The phosphorylation level of His-TF-Rpl12 was detected using an anti-thioP antibody. b, In vitro kinase assays were performed using purified GST-Rpl12 from E. coli as substrates, with purified glucose-starved 3× FLAG-Snf1 or 3× FLAG-Snf1 KD (kinase dead) from yeast cells as protein kinase. The phosphorylation level of GST-Rpl12 was detected using an anti-thioP antibody. c, d, Mass spectrometry identified that residues S79 and S174 of Rpl12 are phosphorylated by Atg1. e, BY4741, 9× MYC-TIR1 cells, rpl12b∆ Rpl12a-AID cells, rpl12b∆ Rpl12a-AID + WT Rpl12a cells, and rpl12b∆ Rpl12a-AID + Rpl12a-2A cells were grown on YPD or YPD supplemented with 0.5 mM IAA agar plate for 2 d at 30 °C. f-i, The indicated yeast cells were treated with IAA for 2 h, and then subjected to SD-N for 0 or 6 h. Ribophagic activity were analyzed by western blot to detect cleavage of GFP-fusion proteins. The results were quantified (see Methods). j, Yeast cells co-expressing either HA-Rpl12 or HA-Rpl12 2 A with GFP-Atg8 were subjected to SD-N for 0 or 1 h. Cell lysates were immunoprecipitated using anti-GFP agarose beads and analyzed by western blot using an anti-HA antibody. k, Ni-NTA pulldown assays were performed using His-TF-Rpl12 or His-TF-Rpl12 2 A with Atg11 CC4 protein from E. Coli. Pgk1 served as a loading control. Blots, gels, and Y2H assays are representatives of three independent experiments. Unprocessed blots/gels are provided in Source data.
Extended Data Fig. 5 Rpl12 is specifically required in yeast ribophagy under starvation conditions.
a, BY4741, atg1Δ, or rpl12bΔ Rpl12a-AID cells expressing either wild-type (WT) Rpl12 or Rpl12S79D-S101D (2D) were grown to the log phase, harvested, and analyzed using an anti-Rpl12 antibody. The data are representative of two independent experiments. b-e, The indicated yeast cells were treated with IAA for 2 h, followed by incubation in SD-N for 0 or 6 h. Ribophagic activity were analyzed by western blot to detect the cleavage of GFP-fusion proteins. f, Ribophagic activity from (b-e) was quantified. g, The indicated yeast cells were treated with IAA for 2 h, then subjected to SD-N for 6 h, followed by performed the APEX-EM analysis. Scale Bar: 500 nm. h, i, The indicated yeast cells expressing Om45-GFP or Pex14-GFP were treated with IAA for 2 h, then subjected to SD-N for 0 or 8 h. Protein samples were analyzed by western blot using an anti-GFP antibody. j, BY4741 cells, atg1∆ cells, or atg39∆ atg40∆ cells expressing with Sec63-GFP were subjected to SD-N for 0 or 8 h. ER-phagy activity was analyzed by western blot using an anti-GFP antibody. k-m, The indicated cells expressing Rpl3-GFP, Rpl25-GFP, or Rps25a-GFP were subjected to SD-N for 0 or 6 h. Ribophagic activity was analyzed by western blot using an anti-GFP antibody. Pgk1 served as a loading control. The data are representatives of three independent experiments unless specified in the legends. Statistical significance: ***P < 0.001, *P < 0.05. P values were calculated by two-tailed Student’s t tests (f) and the data are presented as mean ± s.d. (n = 3 biological replicates). Exact P values, source numerical data and unprocessed blots are provided in Source data.
Extended Data Fig. 6 The Rpl12 P3 and E21 residues are highly conserved across species and rpl-12(sb7750[P3N-E21L]) mutations impair worm growth and development.
a, Amino acid sequence alignment of the RPL12 protein across different species. b, GST pulldown assays were performed using His-TF-RPL-12 protein and GST-LGG-1 or GST-LGG-2 from E. coli. The samples were separated by SDS-PAGE and visualized using Coomassie blue staining. c, Wild-type or cup-5 mutant worms were starved for 0 h or 24 h. Ribosomal protein levels were assessed by western blotting using the indicated antibodies, with Tubulin serving as a loading control. d, Degradation ratios of the indicated proteins from (c) were quantified and presented as mean ± s.d. (n = 3 biological replicates). two-tailed Student’s t tests were used. e, Western blot analysis showing the expression levels of RPL-12-3× FLAG and RPL-12-P3N-E21L-3× FLAG in the indicated worm strains. The data shown are representative of two independent experiments. f, Quantification of the number of normal adult worms per day for each strain(n = 10). All values are presented as mean ± s.d. (n = 3 biological replicates). two-tailed Student’s t tests were used. g, The percentage of embryos that hatched normally into larvae for each strain. (n = 3 biological replicates, 1st repeat: N2 = 722, rpl-12(syb7750) = 654, atg-3(bp412) = 436. 2nd repeat: N2 = 479, rpl-12(syb7750) = 672, atg-3(bp412) = 346. 3rd repeat: N2 = 615, rpl-12(syb7750) = 864, atg-3(bp412) = 490). Two-tailed Student’s t tests were used. h, Lifespan analyses were performed for each strain at 20 °C. P values were calculated using the Log-rank (Mantel-Cox) test (L4440 = 102, atg-3 RNAi = 66, rpl-12 RNAi = 100, rpl-26 RNAi = 90). i, RNAi efficiency was validated by RT-PCR. ama-1 was used as an internal reference gene. Data are shown as mean ± s.d. (n = 3 biological replicates). two-tailed Student’s t tests were used. Blots and gels are representatives of three independent experiments unless specified in the legends. Statistical significance: ***P < 0.001, **P < 0.01, *P < 0.05, ns: no significance. Exact P values, source numerical data and unprocessed blots/gels are provided in Source data.
Extended Data Fig. 7 RPL12 is crucial for maintaining cellular homeostasis in Drosophila.
a, Degradation ratios from Fig. 6d were quantified. b, Ribosomal protein levels were analyzed after treated with chloroquine and starved for 8 h. c, The degradation ratios from (b) were quantified. d, Co-localization of Atg8a with RpL12-3× FLAG or RpL12P3N-E21L(M)- 3× FLAG in muscle tissues. Scale bar: 3 μm(overview) and 1μm (insets: magnified views). e, is the quantitation of d (n = 20). f, Ribosome profiling was analyzed in starved WT and RpL12 P3N-E21L flies’ thorax. g, Sections of fly muscle tissues were stained with hematoxylin and eosin (H&E). Muscle degeneration is indicated by an arrow. Scale bar: 120 μm (overview) and 30 μm (insets: magnified views). h, Actin networks in thorax tissues were analyzed using phalloidin-TRITC staining. Expanded Z-line is indicated. Scale bar: 12 μm (overview) and 7 μm (insets: magnified views). i, is the quantitation of (h) (n = 20). j, RNAi efficiency was validated. k, The levels of ribosomal proteins following starvation treatment. l, is the quantitation of (k). m, Total RNA from HEK293T cells or flies were analyzed. n, rRNA levels were assessed following starvation treatment. o, is the quantitation of (n). p, Starvation sensitivity of the indicated flies. n = 50. q, Climbing abilities of indicated flies under starvation condition (5 groups, n = 10 each). r, Lifespans of indicated flies at 29 °C. n = 50. Tubulin served as a loading control in immunoblot. MHC-Gal4 was used to drive the knockdown and expression of relevant genes in indirect flight muscle (d, j, k, m, p). Data in b, d, g, h, k, m, n are representative of three independent experiments, n = 15 for each replicate in a-c and k-n. P values were calculated by two-tailed Student’s t tests (a, c, e, i, j, l, o, q) and data are are shown as mean ± s.d. The Log-rank (Mantel-Cox) test (p, r) was used to analyze differences in survival rates. Statistical significance: ***P < 0.001, **P < 0.01, ns: no significance. Exact P values, source numerical data, and unprocessed blots are provided in Source data.
Extended Data Fig. 8 Overexpression of RPL12 promotes starvation-induced ribophagy in Drosophila.
a, Age-induced impairment of climbing ability was tested in WT, RpL12, RpL11, Nufip, and Atg5 RNAi flies. Data are shown as mean ± s.d. (5 groups, n = 10 for each group). b-e, Pupation (b), pupa emergence rate (c), as well as lengths of pupa (d) and adult flies (e) were quantified in wild-type (WT), RpL12, RpL11, Nufip, and Atg5 RNAi flies. Data are shown as mean ± s.d. (b, c, 5 groups, n = 20 each; d, e, n = 20). f, Expression levels of RpL12-3×FLAG, RpL12P3N-E21L(M)- 3×FLAG and RpL13-3×FLAG proteins were analyzed by western blot. Data are representative of two independent experiments. g, Climbing abilities of the indicated flies were quantified under starvation conditions. Data are shown as mean ± s.d. (5 groups, n = 10 each). h, Overexpression of wild-type RpL12 mitigates the loss of climbing ability induced by Aβ42. Elav-Gal4 was used to drive overexpression of RpL12, RpL12 P3N-E21L and RpL13 in the fly central nervous system (CNS). Data are shown as mean ± s.d. (4 groups, n = 20 each). i, WT flies and flies overexpressing RpL12-3×FLAG were subjected to starvation for 0 or 4 h. Ribophagic activity was assessed by measuring ribosomal protein levels before and after starvation. j, Degradation ratios from (i) were quantified and presented as mean ± s.d. k, Cell lysates were immunoprecipitated with anti-FLAG agarose beads and analyzed with the indicated antibodies. l, Ribosome profiling was performed in WT and RpL12-OE flies under nutrient-rich conditions. m, n, The fractions isolated from (l) were analyzed by western blot using the indicated antibodies. Tubulin served as a loading control in immunoblot. MHC-Gal4 was used to drive the expression of relevant genes in indirect flight muscle (f, g, k). Data in (i-k, m, n) are representative of three independent experiments, n = 15 for each replicate in f, i-k. P values were calculated by two-tailed Student’s t tests (a-e, g, h, j). ***P < 0.001, **P < 0.01, *P < 0.05, ns: no significance. Exact P values, source numerical data, and unprocessed blots are provided in Source data.
Extended Data Fig. 9 RPL12 regulates ribosome turnover in mammalian cells.
a, HEK293T cells were co-transfected with hRPL12-3×FLAG or hRPL12P3N-E21L-3×FLAG, along with HA-GABARAP or HA-GABARAPL1. The cells were starved with EBSS for 1 h. Cell lysates were immunoprecipitated using anti-HA agarose beads and analyzed by western blot with an anti-FLAG antibody. b, GST pulldown assays were performed using His-TF and His-TF-hRPL12 proteins with GST, GST-LC3s, or GST-GABARAPs expressed in E. coli. c, GST pulldown assays were performed using purified His-TF, His-TF-hRPL12, or His-TF-hRPL12P3N-E21L proteins with GST, GST-LC3C, or GST-GABARAP proteins expressed in E. coli. d, WT and ATG7 KO HEK 293 T cells were starved with EBSS for 0 or 10 h. Western blot analysis assessed protein levels. e, Degradation ratios from (d) were quantified. f, WT and Rpl12 KD stable HEK293T cells were starved for 10 h. and ribophagy activity was assessed by western blot for ribosomal proteins degradation. g, Degradation ratios from (f) were quantified. h, The indicated cell lines were subjected to EBSS starvation for 0 or 10 h, and total RNA was extracted for analysis. i, rRNAs levels from (h) were quantified and normalized to wild-type. j, RPL12 knockdown cells were transfected with the RPL12-3×FLAG plasmid and treated with EBSS alone or EBSS combined with Bafilomycin A1 for 0 or 10 h. Protein samples were analyzed by western blot. k, m, U2OS cells expressing RPL12-3×FLAG were stained with anti-FLAG and anti-ATG14 (k) or anti-ATG16L(m) antibodies after EBSS starvation for 0 or 1 h. Scale bar: 10 μm(overview) and 2 μm (insets: magnified views). l, n, Co-localization of RPL12-3× FLAG with ATG14 (l) or ATG16L (n) (n = 30 cells) were quantified from (k) and (m). Actin and Tubulin served as the loading control. Blots, gels and imaging data are representatives of three independent experiments. Statistical significance: ***P < 0.001, **P < 0.01, ns: no significance. P values were calculated by two-tailed Student’s t tests (e, g, i, l, n) and the data are presented as mean ± s.d. (n = 3 biological replicates). Exact P values, source numerical data and unprocessed blots/gels are provided in Source data.
Extended Data Fig. 10 RPL12 regulates ribosome turnover in mice.
a, HEK293T cells were co-transfected with mRPL12-3×FLAG and HA-tagged mLC3s or mGABARAPs. After EBSS starvation for 1 hour, cell lysates were immunoprecipitated with anti-HA beads and analyzed by western blot with anti-FLAG antibodies. b, HEK293T cells were co-transfected with mRPL12-3×FLAG or mRPL12 P3N-E21L-3× FLAG, along with HA-tagged mLC3A, mLC3B, or mGABARAP. Following EBSS starvation for 1 h. Cell lysates were immunoprecipitated using anti-HA agarose beads and analyzed by western blot with an anti-FLAG antibody. c, GST pulldown assays were conducted using His-TF and His-TF-mRPL12 proteins, along with GST, GST-mLC3s, or GST-mGABARAPs from E. coli. d, GST pulldown assays were performed using His-TF, His-TF-mRPL12, or His-TF-mRPL12 P3N-E21L proteins with GST, GST-mLC3s, or GST-mGABARAP, all purified from E. coli. e, The expression levels of ribosomal and other indicated proteins in the mouse liver under starvation were assessed after intraperitoneal injection with mCherry-tagged rAAV-RPL12-WT or rAAV-RPL12 P3N-E21L (n = 3 mice). f, Degradation ratios from (e) were quantified. g, Total RNA from (e) was analyzed on formaldehyde agarose gels. h, rRNAs levels from (g) were quantified. i, A volcano plot showed MS signal changes in Rpl12 P3N-E21L mutant versus WT liver samples, with red dots (n = 27) indicating significantly changed components |log2FC | > log21.2 and P < 0.01. A two-sided Wald test was conducted without adjustment for multiple comparisons. j, R package DESeq2 (version 1.34.0) was used to identify differentially abundant component in MS from (i), selected by the threshold P < 0.01 and |log2FC | > log21.2. A two-sided Wald test was conducted without adjustment for multiple comparisons. k, l, Blood glucose (k) and hepatic glycogen concentrations (l) under starvation conditions were quantified. Actin and Tubulin served as the loading control. Blots and gels are representatives of three independent experiments. Statistical significance: ***P < 0.001, **P < 0.01, ns: no significance. P values were calculated by two-tailed Student’s t tests (f, h, k, l) and the data are presented as mean ± s.d. (n = 3 biological replicates). Exact P values, source numerical data and unprocessed blots/gels are provided in Source data.
Supplementary information
Supplementary Tables 1–3 and 5 (download XLSX )
MS data showing the interaction between proteins from the yeast lysate treated with nitrogen starvation and GST (Supplementary Table 1), GST–Atg8 (Supplementary Table 2) or GST–Atg8Y49A-L50A protein (Supplementary Table 3), related to Extended Data Fig. 1a, and yeast strains (Supplementary Table 5), related to Figs. 1–4 and Extended Data Figs. 1–5.
Supplementary Table 4 (download XLSX )
Metabolomics results of liver tissues from mice expressing liver-specific WT RPL12 (rAAV-RPL12) or RPL12-P3N-E21L (rAAV-RPL12-P3N-E21L), related to Extended Data Fig. 10i.
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Chen, Y., Hu, J., Zhao, P. et al. Rpl12 is a conserved ribophagy receptor. Nat Cell Biol 27, 477–492 (2025). https://doi.org/10.1038/s41556-024-01598-2
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DOI: https://doi.org/10.1038/s41556-024-01598-2
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