Figure 3.
NLRP1 activation by ribotoxic stress response relies on the ubiquitination machinery and proteasomes. (A–E) HEKNLRP1+ASC (A–C) or N/TERT-1C1C-EGFP cells (D and E) were stimulated with DMSO, 15 µM Aniso (A, C, D, and E), 2 µM Lacti (B, C, and E), or 30 µM Tal (C and E) for the indicated time. Stimulation was performed in the presence of 10 µM Dora, 1 μM MLN7, 1 μM MLN4, 1 μM PF, 200 nM ISRIB, 3 µM Jnk, 20 µM SB, 20 µM BeMeEs, 1 µM MG-132, 1 µM Borte, or DMSO as indicated. N/TERT-1 cells were always stimulated in the presence of 100 µM VX. Specking cells were quantified by flow cytometry as described in Fig. 1. Data represents average values (with individual data points) from three or four independent experiments ± SEM.

NLRP1 activation by ribotoxic stress response relies on the ubiquitination machinery and proteasomes. (A–E) HEKNLRP1+ASC (A–C) or N/TERT-1C1C-EGFP cells (D and E) were stimulated with DMSO, 15 µM Aniso (A, C, D, and E), 2 µM Lacti (B, C, and E), or 30 µM Tal (C and E) for the indicated time. Stimulation was performed in the presence of 10 µM Dora, 1 μM MLN7, 1 μM MLN4, 1 μM PF, 200 nM ISRIB, 3 µM Jnk, 20 µM SB, 20 µM BeMeEs, 1 µM MG-132, 1 µM Borte, or DMSO as indicated. N/TERT-1 cells were always stimulated in the presence of 100 µM VX. Specking cells were quantified by flow cytometry as described in Fig. 1. Data represents average values (with individual data points) from three or four independent experiments ± SEM.

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