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. 2006 Feb 13;172(4):517–528. doi: 10.1083/jcb.200511071

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Copyright © 2006, The Rockefeller University Press

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Figure 1. — Characterization of Dgrip75 depletion by RNAi. (A) Analysis of protein depletion by Western blot. Total protein extracts of control or treated cells (Dgrip75_RNAi) were analyzed using Dgrip75 affinity–purified antibodies and antibodies against Dgrip84, γ-tubulin, or actin (internal loading control). (B) Analysis of protein depletion by immunofluorescence. a and b, microtubules; c and d, Dgrip75 signal. A quantitative view is shown in Table I. (C) Analysis of γ-tubulin complexes after Dgrip75 depletion. Total protein extracts prepared from control or treated cells (Dgrip75_RNAi) were centrifuged in a sucrose gradient. Soluble fractions were analyzed by immunoblotting against γ-TuRC components. (D) Recruitment of γ-TuSC components into the cytoskeletal fraction after Dgrip75 depletion. Total protein extracts (T) of control or treated cells (Dgrip75_RNAi) were centrifuged for 10 min at 10,000 g. Then, the supernatants (S) and the pellets (P) were analyzed by immunoblotting with antibodies against Dgrip91, Dgrip84, γ-tubulin, and Dgrip75. Bar, 5 μm.