Abstract
The Hippo pathway has important roles in organ development, tissue homeostasis and tumour growth. Its downstream effector TAZ is a transcriptional coactivator that promotes target gene expression through the formation of biomolecular condensates. However, the mechanisms that regulate the biophysical properties of TAZ condensates to enable Hippo signalling are not well understood. Here using chemical crosslinking combined with an unbiased proteomics approach, we show that FUS associates with TAZ condensates and exerts a chaperone-like effect to maintain their proper liquidity and robust transcriptional activity. Mechanistically, the low complexity sequence domain of FUS targets the coiled-coil domain of TAZ in a phosphorylation-regulated manner, which ensures the liquidity and dynamicity of TAZ condensates. In cells lacking FUS, TAZ condensates transition into gel-like or solid-like assembles with immobilized TAZ, which leads to reduced expression of target genes and inhibition of pro-tumorigenic activity. Thus, our findings identify a chaperone-like function of FUS in Hippo regulation and demonstrate that appropriate biophysical properties of transcriptional condensates are essential for gene activation.
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Data availability
MS data have been deposited into ProteomeXchange with the identifier PXD040257. Gene expression values were compared with the gene annotation file from GENCODE (v.35). RNA-seq data have been uploaded to the Genome Sequence Archive of The National Genomics Data Center, the China National Center for Bioinformation/Beijing Institute of Genomics and the Chinese Academy of Sciences (accession number PRJCA018564). All other data supporting the findings of this study are available from the corresponding authors upon reasonable request. Source data are provided with this paper.
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Acknowledgements
We thank P. Xia, Y. Zhou, Q. Zhang, W. Huang and staff at the core facility of the Life Sciences Institute for helpful suggestions, discussions and technical assistance. This work was supported in part by the National Natural Science Foundation of China (grants 32070632, 32370591 and 92053114 to H.L., 32270745 to Y.L. and 22074132 to B.Y.), the Zhejiang Provincial Natural Science Foundation of China (grant LR21C060002 to H.L. and LR20B050001 to B.Y.), the National Key R&D Program of China (2022YFF0608402 to B.Y.) and the Fundamental Research Funds for the Central Universities.
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Y.S., Y.L., B.Y. and H.L. designed the research and analysed the data. Y.S., X.S., Y.L., W.Z., R.L., H.F., C.L., W.S., Z.L., Y.Z., X.Y. and E.A. performed the experiments. X.C., B.Z., L.Z., H.W. and X.-.H.F. provided valuable discussions. Y.S., B.Y. and H.L. wrote the paper. B.Y. and H.L. conceived and directed the project. All the authors discussed the results and commented on the paper.
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Extended data
Extended Data Fig. 1 Validation of XL-MS for protein interaction analysis.
a, Schematic depicting the chemical synthesis procedure of L-NHSF. b, Purified recombinant proteins were analyzed by SDS-PAGE and visualized by Coomassie blue staining. c, Purified PRFA and PRMC were untreated or cross-linked with NHSF or L-NHSF and analyzed by Western blotting (WB). d & e, PRFA and PRMC cross-linked with NHSF or L-NHSF were analyzed by mass spectrometry to identify the number of cross-linked peptides (d) and types of cross-linking sites (e). f, Distribution of Cα-Cα distance of cross-linked residues from PRFA and PRMC samples treated with NHSF or L-NHSF. g, GFP-T1-IDR was cross-linked with the indicated concentrations of L-NHSF at 37.5 mM or 150 mM NaCl and analyzed for the formation of droplets. Right: Quantification of GFP-T1-IDR phase separation in the presence of different concentrations of L-NHSF. Data are mean ± SEM. n = 3 biologically independent samples. h, Schematic depicting the crosslinking of GFP-T1-IDR at the indicated NaCl concentrations and then followed by mass spectrometry analysis. i, GFP-TAZ was cross-linked with the indicated concentrations of L-NHSF at 37.5 mM or 150 mM NaCl and analyzed as in g. Bottom: Quantification of the sizes of droplets in the presence of different concentrations of L-NHSF. n = 500 droplets in each group. j, Hela cells expressing WW-F or WW-F plus WW-Strep were subjected to co-immunoprecipitation analysis. Whole cell extract (WCE) and Streptactin immunoprecipitates (IPs) were analyzed by WB. For d, e, f, and i, data are representative of three independent experiments, with similar results obtained.
Extended Data Fig. 2 Reconstituted GFP-TAZ condensates exhibit liquid-like properties and are associated with FUS and several other hits.
a, Time-lapse imaging of GFP-TAZ droplets formed in NE. The arrows indicate the spontaneous fusion event of GFP-TAZ droplets over time. b, Gene Ontology analysis of the MS-identified proteins that preferentially associated with reconstituted GFP-TAZ droplets in NE. c, Cells expressing GFP-TAZ together with mCherry or mCherry-FUS were examined by fluorescence microscopy. DNA was counterstained by Hoechst. Scale bar, 10 μm. d, Cells expressing GFP-TAZ together with mCherry-tagged fusion proteins were examined by fluorescence microscopy. DNA was counterstained by Hoechst. Scale bar, 10 μm.
Extended Data Fig. 3 FUS doesn’t affect Hippo signaling activity and directly inhibits TAZ LLPS.
a, Cells expressing FUS or not were serum-starved for 16 h and then treated with 10% FBS for 1 h. Cell lysates were analyzed by Western blotting (WB) for the indicated proteins. b-d, Control or FUS KD cells were treated as indicated and then analyzed as in a. e, Diagram depicting the protein domains and different FUS variants. f, Percentage of cells that showed GFP-TAZ puncta in cells co-expressed with or without different FUS variants as indicated. Data are mean ± SEM. n = 3 biologically independent samples. g,h, GFP-TAZ mixed with mCherry (g) or mCherry-FUS-LCD (h) at the indicated protein concentrations were analyzed for the formation of droplets at 150 mM NaCl. Scale bar, 50 μm. i, GFP-TAZ mixed with mCherry or mCherry-FUS-LCD at the indicated molar ratio was subjected to droplet co-sedimentation assay and analyzed by WB. S, supernatant; P, pellet. Relative intensities of GFP-TAZ are shown at the bottom.
Extended Data Fig. 4 Phosphorylation of FUS abolishes its association with phase-separated TAZ in a Hippo-independent manner; ALS-linked FUS mutant traps TAZ in the Cytoplasm.
a, The altered residues in FUS mutants are shown. b, GFP-TAZ mixed with NEs prepared from cells expressing indicated FUS mutants was subjected to droplet co-sedimentation assay and analyzed by Western blotting (WB). S, supernatant; P, pellet. c, Cells were untreated or treated with the indicated chemicals. Cell lysates were analyzed by WB for the indicated proteins. d, GFP-TAZ mixed with NEs prepared from cells that were untreated or treated with Calyculin A was subjected to droplet co-sedimentation assay and analyzed as in b. e,f, GFP-TAZ mixed with NEs prepared from cells that were untreated or treated with Calicheamicin and/or DNA-PKi (e) or ATMi (f) as indicated was subjected to droplet co-sedimentation assay and analyzed b. g–i, Lysates collected from cells that are either untreated or treated as indicated were analyzed by WB. j, GFP-TAZ mixed with NEs prepared from cells that were untreated or treated as indicated was subjected to droplet co-sedimentation assay and analyzed as in b. k, Cells transfected with mCherry or mCherry-FUS or mCherry-FUSR521C were immunostained for endogenous TAZ. DNA was counterstained by Hoechst. Scale bar, 10 μm. Insets, regions of the respective panels magnified by 4 times.
Extended Data Fig. 5 Interaction between FUS LCD and TAZ CC domain modulates TAZ phase separation.
a, GFP-FUS-LCD or GFP-LacI-FUS-LCD was co-transfected with BFP-LacI into U2OS-LacO cells. The enrichment of GFP fusions at the LacO array were examined using confocal microscopy. Right: Line plot showing the GFP and BFP fluorescence intensity along the dotted line in the magnified image. b, CC-Flag and CC-Strep were co-transfected with His-mCherry or His-mCherry-FUS-LCD as indicated. Anti-Flag immunoprecipitates (IPs) were analyzed by western blotting. c, Diagram depicting the protein domains and different TAZ chimeras. d, GFP-TAZ mixed with mCherry or mCherry-CCTAZ at the indicated molar ratio was subjected to droplet co-sedimentation assay and analyzed by WB. S, supernatant; P, pellet. Relative intensities of GFP-TAZ are shown at the bottom.
Extended Data Fig. 6 FUS is required for the reversible liquid character of TAZ condensates in cells.
a, Confocal microscopy images of cells expressing GFP-TAZ together with mCherry or mCherry-FUS following different time periods of 1,6-hexanediol treatment. Scale bar, 10 μm. b, Quantification of the percentage of cells showing nuclear puncta as in a. Data are mean ± SEM. n = 3 biologically independent samples. c, Confocal microscopy images of control or FUS KD cells expressing GFP-TAZ following different time periods of 1,6-hexanediol treatment. Scale bar, 10 μm. d, Quantification of the percentage of cells showing nuclear puncta as in c. Data are mean ± SEM. n = 3 biologically independent samples. e, Cells expressing GFP-TAZ together with mCherry-TEAD4, mCherry-CycT1, or mCherry-Brd4 were examined by fluorescence microscopy. Scale bar, 10 μm. f, Cells co-expressing GFP-TAZ along with mCherry-TEAD4, mCherry-CycT1, or mCherry-Brd4 were subjected to FRAP analysis for the mCherry-tagged fusion proteins. Representative images showing the mCherry signals within a TAZ condensate before and at different time points after photobleaching. Scale bar, 1 μm. Data are mean ± SEM. n = 5 biologically independent samples. g, Cells co-expressing mScarlet-TAZ along with GFP-TEAD4 were subjected to FRAP analysis as in f. Representative images showing the GFP signals within a TAZ condensate before and after photobleaching. Scale bar, 1 μm. Data are mean ± SEM. n = 3 biologically independent samples. h, Control or FUS KD cells expressing CFP-TAZ together with YFP-TEAD4 were analyzed by FRET microscopy. The last column shows the normalized FRET images. Bottom: Box plots showing the mean NFRET per nuclei. Scale bar, 10 μm. n = 199 cells, pooled from 3 independent replicates.
Extended Data Fig. 7 FUS promotes TAZ-dependent transcriptional activation.
a, b, 8xGTIIC-Luciferase activity was measured in (a) YAP-expressing cells transfected with mCherry or mCherry-FUS, (b) TAZ- or YAP-expressing cells transfected with mCherry or mCherry-FUS. c, Whole cell extracts (WCEs) of MCF10A or MCF10A-TAZ cells were analyzed by Western blotting (WB) for the indicated proteins. d, h, j, Transcription from the CTGF and CYR61 gene promoters was measured by qRT-PCR in MCF10A or MCF10A-TAZ (d) or MCF10A-TAZ with or without FUS KD (h) or MCF10A-TAZ cells with or without FUS KO (j) cells. e, MCF10A-TAZ cells were subjected to nascent RNA FISH for CYR61, CTGF, and TGFB2 with concurrent immunofluorescence staining with anti-TAZ antibody. DNA was counterstained by DAPI. Insets, regions of the respective panels magnified by 16 times. Scale bar, 10 μm. f, Quantification showing the average TAZ immunofluorescence signal surrounding the FISH foci of CYR61, CTGF, and TGFB2. g, i, Whole cell extracts (WCEs) of MCF10A-TAZ cells with or without FUS KD (g) or FUS KO (i) were analyzed by WB. k, MCF10A or MCF10A-TAZ cells with or without FUS knockdown were examined by RNA-FISH using probes specifically targeting RNA transcripts from CTGF, CYR61, TGFB2, and 18s rRNA, respectively. DNA was counterstained by DAPI. Scale bar, 10 μm. l, MCF10A-TAZ cells with or without FUS KD were serum-starved and then restimulated with serum. Transcription from the CTGF and CYR61 gene promoters was measured by qRT-PCR. m, Box plot showing the fold change in gene expression of TAZ_UP genes and other genes in FUS KD versus control MCF10A-TAZ cells. n = 588 genes examined over 2 independent experiments. n, Heatmap analysis showing the expression profile of TAZ_UP genes in MCF10A-TAZ cells with FUS KD or treated with verteporfin. For experiments in a, b, d, h, j, and l, data are mean ± SEM, n = 3 biologically independent samples.
Extended Data Fig. 8 FUS promotes the oncogenic function of YAP/TAZ.
a, Whole cell extracts (WCEs) of MDA-MB-231 and MDA-MB-231-FUS cells with the individual or double knockout of TAZ and YAP were analyzed by Western blotting (WB) for the indicated proteins. b, Transcription from the CYR61 gene promoters was measured by qRT-PCR in cells as indicated in a. Data are mean ± SEM. n = 3 biologically independent samples. c, Cells as indicated in a were subjected to colony formation assay. Colonies were stained with MTT, quantified, and shown in the graph at the bottom. Data are mean ± SEM. n = 3 biologically independent samples. Scale bar, 7 mm. d, Whole cell extracts (WCEs) of MII-TAZ-4SA cells with or without FUS KD were analyzed by WB. e, Cell growth of MII or MII-TAZ-4SA cells with or without FUS KD was monitored at the indicated times. Data are mean ± SEM. n = 7 biologically independent samples. f, g, i, MCF10A-TAZ (f) or MII-TAZ-4SA (g) cells or MII-TAZ-4SA tumors (i) with or without FUS KD were immunostained for TAZ and then examined using spinning disk confocal microscopy. DNA was counterstained by Hoechst. Scale bar, 10 μm. Insets, regions of the respective panels magnified by 6.3 times (f&g) and 4.6 times (i), respectively. h, MII-TAZ-4SA cells with or without FUS KD were treated with 3 % 1,6-hexanediol for 1 min and then immunostained for TAZ. DNA was counterstained by Hoechst. n = 150 cells, pooled from 3 independent replicates. Scale bar, 10 μm. Right: Quantification of the nuclear TAZ intensity normalized to total TAZ intensity per cell. Red lines indicate the mean value in each group.
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Shao, Y., Shu, X., Lu, Y. et al. A chaperone-like function of FUS ensures TAZ condensate dynamics and transcriptional activation. Nat Cell Biol 26, 86–99 (2024). https://doi.org/10.1038/s41556-023-01309-3
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DOI: https://doi.org/10.1038/s41556-023-01309-3
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