USP10/nsP3 binding to G3BP inhibits B-isox precipitation of G3BP and Caprin1. (A) Tet-on GFP-USP10 cells without (lanes 1–3, 7–9, and 13–15) or with induction (lanes 4–6, 10–12, and 16–18) were treated with AS (500 µM) or CZ (20 µM), or were untreated, before lysis in Kato buffer and B-isox fractionation. Precipitated material (lanes 1–6), input (lanes 7–12), and soluble material (lanes 13–18) were subjected to Western blotting for the indicated proteins. Mr (kD) are shown. (B) U2OS-WT cells stably expressing indicated GFP-tagged proteins were lysed in EE buffer, fractionated using B-isox, and Western blotted for the indicated proteins. SGs or lack thereof are indicated at the bottom. Lanes 1–8, precipitates; lanes 9–11, input; and lanes 12 and 13, soluble material. The C424A USP10 mutant is enzymatically inactive. Mr (kD) are shown.
Figure 6.

USP10/nsP3 binding to G3BP inhibits B-isox precipitation of G3BP and Caprin1. (A) Tet-on GFP-USP10 cells without (lanes 1–3, 7–9, and 13–15) or with induction (lanes 4–6, 10–12, and 16–18) were treated with AS (500 µM) or CZ (20 µM), or were untreated, before lysis in Kato buffer and B-isox fractionation. Precipitated material (lanes 1–6), input (lanes 7–12), and soluble material (lanes 13–18) were subjected to Western blotting for the indicated proteins. Mr (kD) are shown. (B) U2OS-WT cells stably expressing indicated GFP-tagged proteins were lysed in EE buffer, fractionated using B-isox, and Western blotted for the indicated proteins. SGs or lack thereof are indicated at the bottom. Lanes 1–8, precipitates; lanes 9–11, input; and lanes 12 and 13, soluble material. The C424A USP10 mutant is enzymatically inactive. Mr (kD) are shown.

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