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. Author manuscript; available in PMC: 2010 Aug 1.
Published in final edited form as: Nat Cell Biol. 2010 Jan 17;12(2):164–169. doi: 10.1038/ncb2016

Figure 1. Nup107-160 binds γ-TuRC.

Figure 1

(a) 293T cells were co-transfected with plasmids encoding HA-GCP3 and myc-Nup98, myc-Nup96 or myc-Nup107. Immunoprecipitations were performed with anti-myc antibodies or non-specific IgG, and precipitates were subjected to Western blotting with anti-HA antibodies (left panel). A Western blot of input extracts with anti-myc antibodies is shown in the right panel.

(b) Anti-xGCP2 and -xNedd1 antibodies were used for immunoprecipitation from XEEs. In each case, untreated XEE is shown on the left, the precipitated fraction is shown on the right, and the center lane shows proteins eluted from control IgG-coated beads. Uncropped images of the blots are shown in Supplementary Information, Fig. S3.

(c) XEEs were depleted of xNup107-160 using anti-xNup160 antibodies. Co-precipitating proteins (B) and the unbound fraction (U) were analyzed by Western blotting against xNup107-160 or against γ-TuRC components, as indicated. For comparison, similar fractions associated with IgG-coated beads are shown, as well as untreated extracts (Input). Uncropped images of the blots are shown in Supplementary Information, Fig. S3.

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