Protein & Cell

, Volume 10, Issue 11, pp 854–855 | Cite as

Correction to: Developing potent PROTACs tools for selective degradation of HDAC6 protein

  • Zixuan An
  • Wenxing Lv
  • Shang Su
  • Wei WuEmail author
  • Yu RaoEmail author
Open Access

Correction to: Protein Cell

In the original publication the title of X axis in Fig. 1G is incorrectly published as “Compound (µmol/L)”. The correct title of X axis in Fig. 1G should be read as “Compound (nmol/L)”
Figure 1

Development of selective HDAC6-degrading PROTACs. (A) The principle of PROTAC. (B) The structure of PROTAC, as shown in the upper portion. A binding mode of PROTAC (ball stick), HDAC6 (PDB 5G0J, purple) and CRL4-CRBN (PDB 2HYE and 4CI3, colored cyan and gray) was simulated by Pymol. (C) Screen for a potent HDAC6 degrader. HeLa cells were treated as indicated for 24 h. (D) Characterization of NP8-induced degradation in HeLa cells. The degradation of HDAC6 was in a dose-dependent manner. The HDAC1, HDAC2 and HDAC4 levels were not affected within 24 h. (E) NP8 caused fast degradation of HDAC6 within 2 h in HeLa cells. (F) NP8-NC1 and NP8-NC2 failed to degrade HDAC6. NP8 induced degradation was rescued by single introduction of Nexturastat A (Nex A, 300 nmol/L), Pomalidomide (Poma, 10 µmol/L) or Carfilzomib (CARF, 1 µmol/L). The concentration of NP8-NC1, NP8-NC2 and NP8 were 300 nmol/L. HeLa cells were treated with Carfilzomib for 6 h and 24 h for the rest. (G) The degradation of HDAC6 by titration of NP8 for 24 h in MM.1S cells. (H) MM.1S cells were treated with NP8 or Nexturastat A (Nex A) for 72 h. Cell viability was determined by CCK-8 assay (n = 3)

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Authors and Affiliations

  1. 1.MOE Key Laboratory of Protein Sciences, School of Life SciencesTsinghua UniversityBeijingChina
  2. 2.MOE Key Laboratory of Protein Sciences, School of Pharmaceutical Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology, Beijing Advanced Innovation Center for Structural BiologyTsinghua UniversityBeijingChina

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