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. Author manuscript; available in PMC: 2015 Aug 21.
Published in final edited form as: Mol Cell. 2014 Jul 17;55(4):578–591. doi: 10.1016/j.molcel.2014.06.016

Figure 1. Cep192, in a complex with active AurA, recruits multiple PCM proteins.

Figure 1

(A) Fluorescence microscopy of αAurA beads incubated in mock-treated and Cep192-depleted [(-)Cep192] extracts supplemented with rhodamine tubulin and with extract buffer (XB) or the indicated recombinant full-length Cep192 proteins. Scale bar, 5 µm.

(B) Western blot (W-blot) of aAurA beads retrieved from nocodazole-supplemented extracts treated as in (A). Cep192-T46A and Cep192-Δ543–747 are Cep192 mutants lacking the Plx1-docking threonine 46 and the AurA-BD, respectively.

(C) W-blot of M-phase mock-treated and Cep192-depleted extracts supplemented with XB or recombinant full-length Cep192-wt and with sperm nuclei.

(D) Immunofluorescence (IF) of sperm centrioles in extracts treated as in (C) in the absence/presence of nocodazole. Scale bars, 2.5 µm.

(E) W-blot of aAurA beads incubated in mock-treated and AurA-depleted extracts supplemented with XB or the indicated AurA proteins. AurA depletion was performed using a bead-immobilized AurA-binding Cep192 fragment (Cep192521–757), instead of αAurA beads, to prevent co-depletion of endogenous Cep192.

In (B) and (E), the lower panels schematically illustrate bead-protein interactions. W-blots of extracts used in these experiments are shown in Figures S1C and S1D.

See also Figure S1.