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Genes & Development 13: 270-283 (1999)

The SCF^-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IB and -catenin and stimulates IB ubiquitination in vitro

Jefferey T. Winston, Peter Strack, Peggy Beer-Romero, Claire Y. Chu, Stephen J. Elledge, and J. Wade Harper

Figure 3a of the above article was misprinted. The correct figure appears below with its legend in its entirety.

View larger version (95K): [in this window] [in a new window]   Figure 3.   Association of SCF-TRCP with IB and -catenin destruction motifs and with the IB/NF-B complex. (a,b) Cell lysates (0.3 µg of protein/150 µl) from Fig. 2 were used in IB (a) and -catenin (b) peptide bead binding reactions as described in Materials and Methods. Bound proteins were analyzed by immunoblotting with the indicated antibodies. (c) Phosphorylation-dependent association of -TRCPMyc with the IB/p50/p65 complex in vitro. -TRCPMyc immune complexes (lanes 2,5) corresponding to those in Fig. 2a (lane 3) or control complexes (lanes 3,6) corresponding to those in Fig. 2a (lane 1) were used in binding reactions with either IB/p50/p65 or IK- phosphorylated IB/p50/p65 complexes (see Materials and Methods). Bound proteins were separated by SDS-PAGE and immunoblotted using anti-p50 or anti-IB antibodies. The asterisk (lanes 1,4) indicates the positions of 15% of the input IB complexes used in the binding reaction.