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. 2002 Sep 2;158(5):841–847. doi: 10.1083/jcb.200201135

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Copyright © 2002, The Rockefeller University Press

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Figure 1. — Cdc20–GFP complexes with the APC/C proteins Cdc27 and Cdc16 and with spindle checkpoint proteins Mad2 and BubR1 in mitotic HeLa cell extracts. (A) Extracts prepared from cells expressing full-length Cdc20–GFP and blotted with goat anti-Cdc20 antibody show a single band in the immunoprecipitate lane (IP) at ∼82 kD (arrowhead). Endogenous Cdc20 (asterisk) remains in the supernatant (S). (B) Anti-GFP immunoprecipitates from cells expressing full-length Cdc20–GFP or truncated Cdc20–GFP_Δ1–167 show comparable levels of expression. (C) Anti-GFP immunopreciptates from cell extracts expressing full-length Cdc20–GFP contain Mad2, BubR1, Cdc27, and Cdc16. Immunoprecipitates from cell extracts expressing Cdc20–GFP_Δ1–167 lack association with these proteins.

Figure 1. — Cdc20–GFP complexes with the APC/C proteins Cdc27 and Cdc16 and with spindle checkpoint proteins Mad2 and BubR1 in mitotic HeLa cell extracts. (A) Extracts prepared from cells expressing full-length Cdc20–GFP and blotted with goat anti-Cdc20 antibody show a single band in the immunoprecipitate lane (IP) at ∼82 kD (arrowhead). Endogenous Cdc20 (asterisk) remains in the supernatant (S). (B) Anti-GFP immunoprecipitates from cells expressing full-length Cdc20–GFP or truncated Cdc20–GFP_Δ1–167 show comparable levels of expression. (C) Anti-GFP immunopreciptates from cell extracts expressing full-length Cdc20–GFP contain Mad2, BubR1, Cdc27, and Cdc16. Immunoprecipitates from cell extracts expressing Cdc20–GFP_Δ1–167 lack association with these proteins.