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Hsp70 chaperones TDP-43 in dynamic, liquid-like phase and prevents it from amyloid aggregation

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Fig. 1: Hsp70 chaperones TDP-43 in liquid-like phase and prevents it from pathological aggregation.


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This work was supported by grants from the Major State Basic Research Development Program (2019YFE0120600), the Science and Technology Commission of Shanghai Municipality (STCSM) (201409003300, 18JC1420500, 20490712600, 20XD1425000 and 2019SHZDZX02), the National Natural Science Foundation of China (NSFC) (91853113, 81671254, 31872716 and 31970697), and the “Eastern Scholar” project supported by Shanghai Municipal Education Commission. We thank the staff in the National Center for Protein Science, Shanghai, for the assistance on NMR data collection, Ms. J. Hu for help with protein purification, and Drs. C. Zhong, P. Chen and L. He for sharing plasmids.

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YF and CL conceived the research; JG, CW, RH, YF and CL designed the project. JG, CW, RH, YL, SZ and QW performed the experiments; JG, CW, RH, YS and QW contributed important new reagents; JG, CW, RH, YF and CL analyzed the data and interpreted the results; JG, CW and RH prepared the figures; and DL, YF and CL wrote the manuscript. All authors read and approved the final manuscript.

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Correspondence to Yanshan Fang or Cong Liu.

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The authors declare no competing interests.

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Gu, J., Wang, C., Hu, R. et al. Hsp70 chaperones TDP-43 in dynamic, liquid-like phase and prevents it from amyloid aggregation. Cell Res 31, 1024–1027 (2021).

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